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Escherichia coli K-12 substr. MG1655 Protein: Flagellum

Subunit composition of Flagellum = [([FliG]26[FliM]34[FliN])(FlgH)(MotA)(MotB)(FlgB)(FlgC)(FlgF)(FlgG)(FlgI)(FliF)(FliE)][(FlhA)(FlhB)(FliO)(FliP)(FliQ)(FliR)(FliH)12(FliI)6(FliJ)][FlgE]120[FlgK][FlgL][FliC][FliD]5
         Flagellar Motor Complex = ([FliG]26[FliM]34[FliN])(FlgH)(MotA)(MotB)(FlgB)(FlgC)(FlgF)(FlgG)(FlgI)(FliF)(FliE) (extended summary available)
                 Flagellar Motor Switch Complex = (FliG)26(FliM)34(FliN) (extended summary available)
                         flagellar motor switch protein FliG = FliG (summary available)
                         flagellar motor switch protein FliM = FliM (summary available)
                         flagellar motor switch protein FliN = FliN (summary available)
                 flagellar L-ring protein FlgH; basal-body outer-membrane L (lipopolysaccharide layer) ring protein = FlgH (summary available)
                 MotA protein, proton conductor component of motor; no effect on switching = MotA (summary available)
                 MotB protein, enables flagellar motor rotation, linking torque machinery to cell wall = MotB (summary available)
                 flagellar basal-body rod protein FlgB = FlgB (summary available)
                 flagellar basal-body rod protein FlgC = FlgC (summary available)
                 flagellar basal-body rod protein FlgF = FlgF (summary available)
                 flagellar basal-body rod protein FlgG = FlgG (summary available)
                 flagellar P-ring protein FlgI = FlgI (summary available)
                 flagellar M-ring protein FliF; basal-body MS(membrane and supramembrane)-ring and collar protein = FliF (summary available)
                 flagellar basal-body protein FliE = FliE (summary available)
         Flagellar Export Apparatus = (FlhA)(FlhB)(FliO)(FliP)(FliQ)(FliR)(FliH)12(FliI)6(FliJ) (extended summary available)
                 flagellar biosynthesis protein FlhA = FlhA (summary available)
                 flagellar biosynthesis protein FlhB = FlhB (summary available)
                 flagellar biosynthesis protein FliO = FliO (summary available)
                 flagellar biosynthesis protein FliP = FliP (summary available)
                 flagellar biosynthesis protein FliQ = FliQ (summary available)
                 flagellar biosynthesis protein FliR = FliR (summary available)
                 flagellar biosynthesis protein FliH = FliH (summary available)
                 flagellum-specific ATP synthase FliI = FliI (summary available)
                 flagellar biosynthesis protein FliJ = FliJ (summary available)
         flagellar hook protein FlgE = FlgE (summary available)
         flagellar biosynthesis, hook-filament junction protein 1 = FlgK (summary available)
         flagellar biosynthesis; hook-filament junction protein = FlgL (summary available)
         flagellar biosynthesis; flagellin, filament structural protein = FliC (summary available)
         flagellar cap protein FliD; filament capping protein; enables filament assembly = FliD (summary available)

Summary:
The flagellum is a molecular machine with a proton motive force driven rotary motor which rotates a long, curved filament allowing the cell to swim in a liquid environment. Some of the evidence for the structure and function of the flagellum comes from experiments involving Salmonella typhiumurium flagella; however, this evidence is generally believed to apply to the homologous system in E. coli as well.

The three major components of the flagellum are the basal body located within the membranes, and the hook and filament which extend from the basal body outward. The basal body contains the Flagellar Motor Complex and the Flagellar Export Apparatus. The hook is a polymer of FlgE proteins connected to the rod of the basal body. The filament is a polymer of FliC proteins joined to the hook by the FlgK and FlgL hook-filament junction proteins and capped by the filament capping protein, FliD.

The FlgE subunits form 11 parallel rows or protofilaments on the hook's cylindrical surface. Two hook filament junction proteins, FlgK and FlgL, join the hook to the filament [Berg03]. FlgK and FlgL are exported from the cytoplasm with the help of the chaperone FlgN [Fraser99b, Bennett01] via the type III flagellar export apparatus once hook assembly is complete [Kutsukake94].

The 20,000 or so FliC subunits form 11 parallel rows or protofilaments on the filament's cylindrical surface. There are two packing configurations which result in either a left- or a right-handed helical orientation depending on whether the subunits are packed into "long" or "short" protofilaments, respectively. If both types of protofilaments are present simultaneously, the helical filament has both curvature as well as twist with the short protofilaments aligned along the inside of the helix. Each filament is driven at a rotational speed of around 100 Hz by a membrane-embedded rotary motor at its base capable of switching direction of rotation in response to signals from the chemotaxis system. Flagellar/motor complexes are located peritrichously around the outside of the cell with 4, on average, per cell. They originate at random points on its sides and extend several cell body lengths out into the medium. During smooth swimming, their rotation is counterclockwise, causing the flagella to bundle together and propel the cell forward. When the flagellar motor switches to clockwise, the filament's helical orientation transforms from a left-handed supercoil to a right-handed supercoil. The transformation first occurs at the base of the filaments and propagates quickly to the distal end causing the filament bundles to fall apart smoothly which results in tumbling. The run usually lasts for a few seconds followed by the tumble for a fraction of a second. The flagellar filament is connected proximally to a flexible hook structure which is a polymer of FlgE subunits, via two hook-filament junction proteins (FlgK and FlgL) and distally to the flagellar cap, FliD [Hasegawa98, Berg03, Samatey01].

The cap complex consists of five subunits of FliD, which form a pentagonal plate domain and axially extended leg-like domains which insert into cavities at the distal end of the growing filament [Maki98]. The resulting space formed under the cap plate serves as a folding chamber for the FliC flagellin subunits that have just been exported to the distal end of the nascent flagella [Yonekura00]. The leg-like domains of the flagellar cap allow for limited flexibility, permitting insertion of newly folded FliC into an indentation or open gap caused by a symmetry mismatch between the cap and the filament's distal end [Yonekura00]. Upon incorporation of a FliC monomer into the indentation, the cap complex rotates and moves up through conformational rearrangement of the leg-like domains. This creates a new open gap indentation which serves as the next flagellin binding site [MakiYonekura03, Minamino04].

Gene-Reaction Schematic: ?

Credits:
Created 31-Oct-2006 by Johnson A , TIGR


Subunit of Flagellum: Flagellar Motor Complex

Summary:
The bacterial flagellar motor of Escherichia coli is a complex of about 20 different parts no more than 50 nm in diameter. It is capable of spinning clockwise (CW) or counterclockwise (CCW) at speeds approaching 100 Hz, propelling the corkscrew shaped flagellar filaments (FliC subunits) and generating motion. E. coli are peritrichously flagellated (peri, around, trichos, hair) with usually four motor/filament structures arranged randomly around the sides of the cell and extending out several body lengths. When the motors turn CCW, the filaments bundle together in a coordinated effort which pushes the cell steadily forward in a "run". Conversely, when the direction of motor rotation is switched to CW, the coordination of the flagellar bundle is disrupted and the cell tumbles randomly and then starts out in a new direction based on concentrations of attractants or repellents which control the motor switching mechanism [Berg03]. Flagella motors also adapt to mechanical stimuli (ie. sudden changes in load) by changing their speed and CW bias [Lele13].

The bacterial flagellar motor core is made up of a complex group of protein constituents. There are four rod proteins (FlgB, FlgC, FlgF and FlgG) and three ring proteins (FlgH, FlgI and FliF) which form the L, P and MS rings, respectively. These three rings, through which the rod passes, are embedded in the cell wall. The outer two rings, L (FlgH) and P (FlgI), are spaced apart and linked by a cylindrical wall. The inner two rings, S and M, are in direct contact and comprise a single protein (FliF) known as the "MS ring". The three rings, according to their known biochemical and geometrical properties, occupy distinct locations within the intact cell, with the L ring in the plane of the outer lipopolysaccharide membrane, the P ring in the plane of the peptidoglycan layer and the MS ring (membrane/supramembrane) in and above the cell membrane [Berg03].

The MS ring is the first substructure of the flagellar structure to be assembled and serves as the base structure for bacterial flagellar assembly and to anchor the flagellum in the cytoplasmic membrane [Grunenfelder03, Suzuki98a]. There are about 26 copies of FliF monomer in each MS (membrane and supramembrane) ring complex [Sosinsky92]. The complex consists of the MS rings as well as a proximal portion of the rod in the flagellar basal body [Suzuki98a]. FliF is firmly attached to the distal side of FliG, which interacts with the stator protein complex to generate torque [Suzuki04b]. Assembly of the MS ring can occur in the absence of any of the other components of the flagellar structure [Katayama96] and the subsequent distal structural components (with the exception of the P and the L rings) are assembled via single-file export through the MS ring structure coupled with the transport apparatus complex of proteins [Macnab03]. This type of export is termed the flagellar-specific type III secretion system and it is highly similar in appearance and sequence homology to the type III pathways used for virulence secretion. The P and L rings are exported through the primary, or Sec, pathway [Macnab03].

FliE is a component of the basal body assembly. FliE has been shown to physically interact with FlgB and is thought to be a structural adapter between the FliF (MS) ring and the rod, a rotational component which is situated transverse to the outer membrane and peptidoglycan layers [Minamino00].

FlgB, FlgC, FlgF, and FlgG are four proteins that comprise the rod section of the basal-body assembly of the flagellar motor. The rod is a rotational component which is situated transverse to the outer membrane and peptidoglycan layers and is circumscribed by a set of four rings which lie in a horizontal plane within the inner and outer membranes of the cell envelope. The rod acts as a drive shaft to transmit torque from the motor through the flexible hook to the flagellar filament thus allowing for bacterial locomotion [Jones90]. FlgG is a distal component of the basal body rod [SaijoHamano04, Berg03].

FliM and FliN make up the C-ring, which is located inside (cytoplasmic) the cell. Together with FliG, FliM and FliN make up the switch complex which is essential for assembly, rotation and directional control [Welch93]. Although at least one study [Thomas99a] suggests that the MS and C rings rotate relative to one another, the consensus seems to be that the MS and the C-rings rotate as a unit, and together form the rotor of the motor. Mutation deletion studies of the fliG, fliM and fliN [Yamaguchi86] resulted in defects in motor rotation control.

MotA and MotB are thought to form a torque-generating stator complex. MotA and MotB have shown to co-isolate in binding studies [Tang96]. MotA and MotB are membrane embedded and do not fractionate with the other hook-basal body proteins [Ridgway77]. Both proteins span the cytoplasmic membrane with MotA having four membrane-spanning alpha-helical segments and about two-thirds of its mass in the cytoplasm [Blair91, Zhou95]. MotB has one membrane-spanning alpha-helix but the majority of the molecule is in the periplasmic space with a peptidoglycan-binding domain near its C-terminus [Chun88]. MotB is thought to anchor MotA to the cell wall's rigid framework, allowing the MotA/MotB complex to serve as the stationary stator of the flagellar motor [Berg03]. Mutations in MotB near the region where it is thought to be bound to the peptidoglycan region result in the apparent misalignment of the stator and rotor [Garza96]. MotA and MotB are arranged in a circular fashion around the MS and C-rings. In freeze-fracture electron microscopy, MotA and MotB can be visualized as circular "ring particles" or "studs" lying in a plane within the inner membrane of Escherichia coli [Khan88a]. The stoichiometric composition per motor has been determined as being MotA4 MotB2 [Kojima04, Braun04]. Studies using GFP-labeled MotB revealed 11 stators per motor complex, each composed of two copies of MotB and four copies of MotA [Reid06, Leake06]. Direct observation of rotation steps in a Na+-driven chimaeric flagellar motor supports the evidence for 11 stators per motor complex [Sowa05]. The results from cross-linking studies have been used to examine the organization of some transmembrane helices in MotA and MotB and to develop a model for the overall organization of the entire MotA-MotB complex [Kim08e].

The MotA/MotB complex conducts protons across the membrane and then couples this proton flow to rotational torque of the motor [Kojima04] in a process that involves the protonation/deprotonation of the Asp32 residue of MotB [Zhou98a, Braun01]. Two proton channels are formed per complex, with two copies of MotA forming eight transmembrane segments and one additional transmembrane segment coming from one copy of MotB [Braun04]. Mutation suppression studies of motA and motB [Garza96a, Garza95] indicate that MotA and MotB may interact with each other as well as with FliG (which is located at the cytoplasmic face at the periphery of the MS-ring and is thought to comprise part of the rotor of the flagellar motor). Charged residues have been defined in MotA's cytoplasmic domain which are critical for interaction with oppositely charged groups in the C-terminal domain of FliG [Zhou97a, Zhou98b, Yakushi06]. The electrostatic interactions between these pairs of charged groups at the rotor-stator interface are thought to play a significant role in torque generation. The torque necessary for flagellar rotation, then, is apparently generated by the protonation and deprotonation of Asp32 of MotB, which then results in a conformational modulation of MotA. This results in an alteration in the interactions between a specific charged region of MotA's cytoplasmic domain and a complementary charged region in the C-terminal domain of FliG [Berg03].

Deletion mutation studies [Macnab92] have shown that FliG, FliM, FliN, MotA and MotB are the only proteins that function specifically in motor rotation since mutations in only these proteins result in cessation of rotation but not in flagellar assembly.

Reviews: [Morimoto14]


Subunit of Flagellar Motor Complex: Flagellar Motor Switch Complex

Summary:
FliG, FliM, and FliN are the three components of the flagellar motor's "switch complex," and are essential for motor assembly, rotation, and switching. The flagellar motor switch complex binds to the stator elements anchored in the membrane through interactions between FliG of the switch complex and the MotA protein of the stators. The motor switch is also bound to the MS ring through interactions between FliG and the MS ring protein FliF. FliG, FliM, and FliN form the C ring of the flagellum.

There are predicted to be 26 molecules of FliG, 34 of FliM, and greater than 100 of FliN per motor complex [Lowder05, Paul06a]. Direct observation of rotation steps in a Na+-driven chimaeric flagellar motor supports the evidence for 26 molecules each of FliG per motor complex [Sowa05]. Targeted cross-linking studies reveal FliN exits as a doughnut-shaped tetramer bound to a single FliM molecule [Paul06a]. Yeast two-hybrid experiments identify interactions between FliF/FliG, FliG/FliM, FliM/FliM, and FliM/FliN pairs [Marykwas96, Marykwas96a]. Affinity blotting and chemical crosslinking experiments confirm the FliG/FliM and FliM/FliN interactions and identify FliM/CheY-P interactions [Toker97, Bren98]. Suppressor mutations indicate the FliM/FliG interaction site and suggest that two FliM molecules are present as a dimer per molecule of FliG [Passmore08].

The interaction between FliM and CheY-P allows the signal transduction system to induce a "switch" from counterclockwise to clockwise rotation of the flagella in response to chemical signals by causing a conformational change in FliM that is transmitted to FliG [Bren98]. Flagellar switching has been modelled using both a two-state, on-off mechanism in which switch events are instantaneous [Alon98], and a conformational spread mechanism in which switch events show a broadly distributed duration and incomplete switching is prevalent [Duke01, Bai10]. Many deletion mutations in the genes expressing the three components of the motor switch complex result in defects in switching [Yamaguchi86a].

The proteins of the flagellar motor switch complex are also involved in flagellar assembly because null mutations are non-flagellate. FliN is responsible for binding of substrate-bound cytosolic components of the flagellar export apparatus to direct them to the membrane components for export of the substrate. Co-purification studies reveal complexes of FliG, FliM, FliN, FliH, and FliI [GonzalezPedrajo06]. FliN was shown to bind FliH in a manner that does not disrupt the FliM/FliN and FliH/FliI interactions. FliM has also been shown to bind FliJ, a general chaperone for flagellar proteins exported through the export apparatus, though this interaction weakens FliM/FliN and FliN/FliH interactions [GonzalezPedrajo06].


Subunit of Flagellar Motor Switch Complex: flagellar motor switch protein FliG

Synonyms: FliG

Gene: fliG Accession Numbers: EG11654 (EcoCyc), b1939, ECK1937

Locations: inner membrane, cell projection

Sequence Length: 331 AAs

Molecular Weight: 36.776 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0044780 - bacterial-type flagellum assembly Inferred from experiment [Lloyd96]
GO:0071973 - bacterial-type flagellum-dependent cell motility Inferred from experiment Inferred by computational analysis [GOA01a, Lloyd96]
GO:0006935 - chemotaxis Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
GO:0097588 - archaeal or bacterial-type flagellum-dependent cell motility Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Hauser14, Rajagopala14, Paul11, Rajagopala09, Paul10, Marykwas96a, Marykwas96, Brown07]
GO:0042802 - identical protein binding Inferred from experiment [Paul11, Paul10]
GO:0003774 - motor activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Zhang07, LopezCampistrou05]
GO:0009288 - bacterial-type flagellum Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0009425 - bacterial-type flagellum basal body Inferred by computational analysis [UniProtGOA11]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
metabolism biosynthesis of macromolecules (cellular constituents) flagellum

Unification Links: EcoliWiki:b1939 , Mint:MINT-8213365 , ModBase:P0ABZ1 , PR:PRO_000022658 , Protein Model Portal:P0ABZ1 , RefSeq:NP_416449 , SMR:P0ABZ1 , String:511145.b1939 , UniProt:P0ABZ1

Relationship Links: InterPro:IN-FAMILY:IPR000090 , InterPro:IN-FAMILY:IPR011002 , InterPro:IN-FAMILY:IPR028263 , Panther:IN-FAMILY:PTHR30534 , Pfam:IN-FAMILY:PF01706 , Pfam:IN-FAMILY:PF14842 , Prints:IN-FAMILY:PR00954

Summary:
FliG is one of three components of the flagellar motor's "switch complex." The crystal structure of the middle and C-terminals of the FliG protein in Thermotoga maritima has been determined to 3.3 A resolution [Brown02b]. The amino terminal region is suggested to be required for flagellar assembly while the carboxy-terminal region is required for torque generation [Van04c], and contains charged residues which interact with MotA. Single residue substitutions within the "hinge" region linking these two domains result in a number of different phenotypes such as rotational biases, altered switching frequencies, and reduced torque generation [Van04c]. Targeted cross-linking studies provide a model for FliG organization within the flagellum [Lowder05].

Essentiality data for fliG knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellar Motor Switch Complex: flagellar motor switch protein FliM

Synonyms: FlaA, Fla, FlaQ, FliM

Gene: fliM Accession Numbers: EG10323 (EcoCyc), b1945, ECK1943

Locations: inner membrane, cell projection

Sequence Length: 334 AAs

Molecular Weight: 37.849 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006935 - chemotaxis Inferred by computational analysis [UniProtGOA11a]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
GO:0071973 - bacterial-type flagellum-dependent cell motility Inferred by computational analysis [GOA01a]
GO:0097588 - archaeal or bacterial-type flagellum-dependent cell motility Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Hauser14, Rajagopala14, Paul11, Rajagopala09, Paul10, Marykwas96]
GO:0003774 - motor activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0009288 - bacterial-type flagellum Inferred by computational analysis [UniProtGOA11a]
GO:0009425 - bacterial-type flagellum basal body Inferred by computational analysis [UniProtGOA11, GOA01a]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
metabolism biosynthesis of macromolecules (cellular constituents) flagellum

Unification Links: DIP:DIP-1100N , EcoliWiki:b1945 , Mint:MINT-1301311 , ModBase:P06974 , PR:PRO_000022664 , Pride:P06974 , Protein Model Portal:P06974 , RefSeq:NP_416455 , SMR:P06974 , String:511145.b1945 , UniProt:P06974

Relationship Links: InterPro:IN-FAMILY:IPR001543 , InterPro:IN-FAMILY:IPR001689 , PDB:Structure:1F4V , PDB:Structure:1U8T , PDB:Structure:2B1J , Pfam:IN-FAMILY:PF01052 , Pfam:IN-FAMILY:PF02154 , Prints:IN-FAMILY:PR00955

Summary:
FliM is one of three components of the flagellar motor's "switch complex." Expression of fliM is upregulated by ZnSO4 in the medium, and a fliM mutant is hypersensitive to ZnSO4 [Lee05].

Essentiality data for fliM knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellar Motor Switch Complex: flagellar motor switch protein FliN

Synonyms: MotD, FliN

Gene: fliN Accession Numbers: EG10324 (EcoCyc), b1946, ECK1944

Locations: inner membrane, cell projection

Sequence Length: 137 AAs

Molecular Weight: 14.855 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006935 - chemotaxis Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
GO:0071973 - bacterial-type flagellum-dependent cell motility Inferred by computational analysis [GOA01a]
GO:0097588 - archaeal or bacterial-type flagellum-dependent cell motility Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Hauser14, Rajagopala14, Rajagopala09, Marykwas96]
GO:0003774 - motor activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09]
GO:0009288 - bacterial-type flagellum Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0009425 - bacterial-type flagellum basal body Inferred by computational analysis [UniProtGOA11, GOA01a]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
metabolism biosynthesis of macromolecules (cellular constituents) flagellum

Unification Links: DIP:DIP-1101N , EcoliWiki:b1946 , ModBase:P15070 , PR:PRO_000022665 , Protein Model Portal:P15070 , RefSeq:NP_416456 , SMR:P15070 , String:511145.b1946 , Swiss-Model:P15070 , UniProt:P15070

Relationship Links: InterPro:IN-FAMILY:IPR001172 , InterPro:IN-FAMILY:IPR001543 , InterPro:IN-FAMILY:IPR012826 , Pfam:IN-FAMILY:PF01052 , Prints:IN-FAMILY:PR00956

Summary:
FliN, is one of three components of the flagellar motor's "switch complex." The crystal structure of the C-terminal domain of the FliN protein in Thermotoga maritime has been determined to 3.4 Å resolution [Brown05].

Essentiality data for fliN knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellar Motor Complex: flagellar L-ring protein FlgH; basal-body outer-membrane L (lipopolysaccharide layer) ring protein

Synonyms: FlaY, FlgH

Gene: flgH Accession Numbers: G364 (EcoCyc), b1079, ECK1064

Locations: outer membrane, cell projection

Sequence Length: 232 AAs

Molecular Weight: 24.615 kD (from nucleotide sequence)

Molecular Weight: 26 kD (experimental) [Jones87b]

GO Terms:

Biological Process: GO:0006970 - response to osmotic stress Inferred from experiment [Krisko14]
GO:0001539 - cilium or flagellum-dependent cell motility Inferred by computational analysis [GOA06]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
GO:0071973 - bacterial-type flagellum-dependent cell motility Inferred by computational analysis [GOA01a]
Molecular Function: GO:0003774 - motor activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0009279 - cell outer membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06, DiazMejia09]
GO:0009288 - bacterial-type flagellum Inferred by computational analysis [UniProtGOA11a]
GO:0009425 - bacterial-type flagellum basal body Inferred by computational analysis [UniProtGOA11]
GO:0009427 - bacterial-type flagellum basal body, distal rod, L ring Inferred by computational analysis [GOA01a]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
metabolism biosynthesis of macromolecules (cellular constituents) flagellum

Unification Links: EcoliWiki:b1079 , Pride:P0A6S0 , Protein Model Portal:P0A6S0 , RefSeq:NP_415597 , String:511145.b1079 , UniProt:P0A6S0

Relationship Links: InterPro:IN-FAMILY:IPR000527 , Pfam:IN-FAMILY:PF02107 , Prints:IN-FAMILY:PR01008 , Prosite:IN-FAMILY:PS51257

Summary:
FlgH is the basic subunit which makes up the L or lipopolysaccharide ring of the flagellar basal body. The L ring lies in the plane of the outer membrane and encircles the basal body rod [Berg03].

flgH shows differential codon adaptation, resulting in differential translation efficiency signatures, in halophilic microbes. It was therefore predicted to play a role in the osmotic stress response. An flgH deletion mutant was shown to be more sensitive than wild-type specifically to osmotic stress, but not other stresses [Krisko14].

Essentiality data for flgH knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellar Motor Complex: MotA protein, proton conductor component of motor; no effect on switching

Synonyms: FlaJ, MotA

Gene: motA Accession Numbers: EG10601 (EcoCyc), b1890, ECK1891

Locations: inner membrane

Sequence Length: 295 AAs

Molecular Weight: 32.011 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0071973 - bacterial-type flagellum-dependent cell motility Inferred from experiment [Wilson88a]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11a]
GO:0006935 - chemotaxis Inferred by computational analysis [UniProtGOA11a]
GO:0015031 - protein transport Inferred by computational analysis [GOA01a]
GO:0015992 - proton transport Inferred by computational analysis [UniProtGOA11a]
GO:0097588 - archaeal or bacterial-type flagellum-dependent cell motility Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0008565 - protein transporter activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Zhang07, Daley05, Wilson88a]
GO:0016021 - integral component of membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Wilson88a]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure membrane
transport Channel-type Transporters alpha-type channels

Unification Links: DIP:DIP-10244N , EcoliWiki:b1890 , Mint:MINT-1250843 , PR:PRO_000023274 , Protein Model Portal:P09348 , RefSeq:NP_416404 , String:511145.b1890 , UniProt:P09348

Relationship Links: InterPro:IN-FAMILY:IPR000540 , InterPro:IN-FAMILY:IPR002898 , InterPro:IN-FAMILY:IPR022522 , Pfam:IN-FAMILY:PF01618 , Prosite:IN-FAMILY:PS01307

Summary:
MotA and MotB comprise the stator element of the flagellar motor complex.

Essentiality data for motA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellar Motor Complex: MotB protein, enables flagellar motor rotation, linking torque machinery to cell wall

Synonyms: FlaJ, MotB

Gene: motB Accession Numbers: EG10602 (EcoCyc), b1889, ECK1890

Locations: inner membrane

Sequence Length: 308 AAs

Molecular Weight: 34.186 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006935 - chemotaxis Inferred by computational analysis [UniProtGOA11a]
GO:0097588 - archaeal or bacterial-type flagellum-dependent cell motility Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, Wilson90]
GO:0016021 - integral component of membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Wilson90]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
cell structure membrane
transport Channel-type Transporters alpha-type channels

Unification Links: DIP:DIP-47996N , EcoliWiki:b1889 , ModBase:P0AF06 , PR:PRO_000023275 , Pride:P0AF06 , Protein Model Portal:P0AF06 , RefSeq:NP_416403 , SMR:P0AF06 , String:511145.b1889 , UniProt:P0AF06

Relationship Links: InterPro:IN-FAMILY:IPR006665 , InterPro:IN-FAMILY:IPR025713 , Pfam:IN-FAMILY:PF00691 , Pfam:IN-FAMILY:PF13677 , Prosite:IN-FAMILY:PS51123

Summary:
MotB and MotA comprise the stator element of the flagellar motor complex.

Essentiality data for motB knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellar Motor Complex: flagellar basal-body rod protein FlgB

Synonyms: FlbA, FlgB

Gene: flgB Accession Numbers: G358 (EcoCyc), b1073, ECK1058

Locations: periplasmic space, cell projection

Sequence Length: 138 AAs

Molecular Weight: 15.24 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0071973 - bacterial-type flagellum-dependent cell motility Inferred by computational analysis [GOA01a]
Cellular Component: GO:0009288 - bacterial-type flagellum Inferred by computational analysis [UniProtGOA11a]
GO:0009425 - bacterial-type flagellum basal body Inferred by computational analysis [UniProtGOA11, GOA01a]
GO:0030288 - outer membrane-bounded periplasmic space Inferred by computational analysis [DiazMejia09]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
metabolism biosynthesis of macromolecules (cellular constituents) flagellum

Unification Links: EcoliWiki:b1073 , PR:PRO_000022638 , Protein Model Portal:P0ABW9 , RefSeq:NP_415591 , String:511145.b1073 , UniProt:P0ABW9

Relationship Links: InterPro:IN-FAMILY:IPR001444 , InterPro:IN-FAMILY:IPR006300 , InterPro:IN-FAMILY:IPR019776 , Pfam:IN-FAMILY:PF00460 , Prosite:IN-FAMILY:PS00588

Summary:
FlgB is one of four protein that comprise the rod section of the basal-body assembly of the flagellar motor [Jones90].

Essentiality data for flgB knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellar Motor Complex: flagellar basal-body rod protein FlgC

Synonyms: FlaW, FlgC

Gene: flgC Accession Numbers: G359 (EcoCyc), b1074, ECK1059

Locations: periplasmic space, cell projection

Sequence Length: 134 AAs

Molecular Weight: 13.968 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0071973 - bacterial-type flagellum-dependent cell motility Inferred by computational analysis [GOA01a]
Cellular Component: GO:0009288 - bacterial-type flagellum Inferred by computational analysis [UniProtGOA11a]
GO:0009425 - bacterial-type flagellum basal body Inferred by computational analysis [UniProtGOA11]
GO:0030288 - outer membrane-bounded periplasmic space Inferred by computational analysis [DiazMejia09]
GO:0030694 - bacterial-type flagellum basal body, rod Inferred by computational analysis [GOA01a]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
metabolism biosynthesis of macromolecules (cellular constituents) flagellum

Unification Links: EcoliWiki:b1074 , PR:PRO_000022639 , Protein Model Portal:P0ABX2 , RefSeq:NP_415592 , SMR:P0ABX2 , String:511145.b1074 , UniProt:P0ABX2

Relationship Links: InterPro:IN-FAMILY:IPR001444 , InterPro:IN-FAMILY:IPR006299 , InterPro:IN-FAMILY:IPR010930 , InterPro:IN-FAMILY:IPR019776 , Pfam:IN-FAMILY:PF00460 , Pfam:IN-FAMILY:PF06429 , Prosite:IN-FAMILY:PS00588

Summary:
FlgC is one of four proteins that comprise the rod section of the basal-body assembly of the flagellar motor [Jones90].

Essentiality data for flgC knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellar Motor Complex: flagellar basal-body rod protein FlgF

Synonyms: FlaX, FlgF

Gene: flgF Accession Numbers: G362 (EcoCyc), b1077, ECK1062

Locations: cell projection

Sequence Length: 251 AAs

Molecular Weight: 25.912 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0071973 - bacterial-type flagellum-dependent cell motility Inferred by computational analysis [GOA01a]
Cellular Component: GO:0009288 - bacterial-type flagellum Inferred by computational analysis [UniProtGOA11a]
GO:0009425 - bacterial-type flagellum basal body Inferred by computational analysis [UniProtGOA11]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
metabolism biosynthesis of macromolecules (cellular constituents) flagellum

Unification Links: EcoliWiki:b1077 , PR:PRO_000022642 , Protein Model Portal:P75938 , RefSeq:NP_415595 , String:511145.b1077 , UniProt:P75938

Relationship Links: InterPro:IN-FAMILY:IPR001444 , InterPro:IN-FAMILY:IPR010930 , InterPro:IN-FAMILY:IPR019776 , InterPro:IN-FAMILY:IPR020013 , Pfam:IN-FAMILY:PF00460 , Pfam:IN-FAMILY:PF06429 , Prosite:IN-FAMILY:PS00588

Summary:
FlgF is one of four proteins that comprise the rod section of the basal-body assembly of the flagellar motor [Jones90].

Essentiality data for flgF knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellar Motor Complex: flagellar basal-body rod protein FlgG

Synonyms: FlaL, FlgG

Gene: flgG Accession Numbers: G363 (EcoCyc), b1078, ECK1063

Locations: outer membrane, cell projection

Sequence Length: 260 AAs

Molecular Weight: 27.744 kD (from nucleotide sequence)

Molecular Weight: 27 kD (experimental) [Komeda78]

GO Terms:

Biological Process: GO:0006928 - cellular component movement Inferred by computational analysis [GOA01a]
GO:0044781 - bacterial-type flagellum organization Inferred by computational analysis [GOA01a]
GO:0071973 - bacterial-type flagellum-dependent cell motility Inferred by computational analysis [GOA01a]
Cellular Component: GO:0009279 - cell outer membrane Inferred from experiment [LopezCampistrou05]
GO:0009288 - bacterial-type flagellum Inferred by computational analysis [UniProtGOA11a]
GO:0009425 - bacterial-type flagellum basal body Inferred by computational analysis [UniProtGOA11]
GO:0009426 - bacterial-type flagellum basal body, distal rod Inferred by computational analysis [GOA01a]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
metabolism biosynthesis of macromolecules (cellular constituents) flagellum

Unification Links: EcoliWiki:b1078 , PR:PRO_000022643 , Pride:P0ABX5 , Protein Model Portal:P0ABX5 , RefSeq:NP_415596 , SMR:P0ABX5 , String:511145.b1078 , UniProt:P0ABX5

Relationship Links: InterPro:IN-FAMILY:IPR001444 , InterPro:IN-FAMILY:IPR010930 , InterPro:IN-FAMILY:IPR012834 , InterPro:IN-FAMILY:IPR019776 , InterPro:IN-FAMILY:IPR020013 , Pfam:IN-FAMILY:PF00460 , Pfam:IN-FAMILY:PF06429 , Prosite:IN-FAMILY:PS00588

Summary:
FlgG is one of four proteins that comprise the rod section of the basal-body assembly of the flagellar motor [Jones90].

Essentiality data for flgG knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellar Motor Complex: flagellar P-ring protein FlgI

Synonyms: FlaM, FlgI

Gene: flgI Accession Numbers: G365 (EcoCyc), b1080, ECK1065

Locations: periplasmic space, cell projection

Sequence Length: 365 AAs

Molecular Weight: 38.169 kD (from nucleotide sequence)

Molecular Weight: 38 kD (experimental) [Komeda78]

GO Terms:

Biological Process: GO:0006974 - cellular response to DNA damage stimulus Inferred from experiment [Khil02]
GO:0001539 - cilium or flagellum-dependent cell motility Inferred by computational analysis [GOA06]
GO:0071973 - bacterial-type flagellum-dependent cell motility Inferred by computational analysis [GOA01a]
Molecular Function: GO:0005198 - structural molecule activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0009288 - bacterial-type flagellum Inferred by computational analysis [UniProtGOA11a]
GO:0009425 - bacterial-type flagellum basal body Inferred by computational analysis [UniProtGOA11]
GO:0009428 - bacterial-type flagellum basal body, distal rod, P ring Inferred by computational analysis [GOA01a]
GO:0030288 - outer membrane-bounded periplasmic space Inferred by computational analysis [GOA01a, DiazMejia09]
GO:0042597 - periplasmic space Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
metabolism biosynthesis of macromolecules (cellular constituents) flagellum

Unification Links: DIP:DIP-47979N , EcoliWiki:b1080 , PR:PRO_000022644 , Pride:P0A6S3 , Protein Model Portal:P0A6S3 , RefSeq:NP_415598 , String:511145.b1080 , UniProt:P0A6S3

Relationship Links: InterPro:IN-FAMILY:IPR001782 , Pfam:IN-FAMILY:PF02119 , Prints:IN-FAMILY:PR01010

Summary:
FlgI is the basic subunit which makes up the P or peptidoglycan ring of the flagellar basal body. The P ring lies in the plane of the peptidoglycan layer and encircles the basal body rod [Berg03]. Experiments with Salmonella typhimurium show FlgI is translocated to the periplasmic space by the Sec translocase [Homma87] where FlgA acts as a chaperone in assembly of the P ring [Nambu00]. FlgI contains an intramolecular disulfide bond which functions in preventing degradation of the protein in the periplasmic space [Hizukuri06]. The highly conserved N-terminal region of FlgI is speculated to play an important role in stabilisation of FlgI and in formation of the P ring [Hizukuri08].

Essentiality data for flgI knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellar Motor Complex: flagellar M-ring protein FliF; basal-body MS(membrane and supramembrane)-ring and collar protein

Synonyms: FliF

Gene: fliF Accession Numbers: EG11347 (EcoCyc), b1938, ECK1936

Locations: inner membrane, cell projection

Sequence Length: 552 AAs

Molecular Weight: 60.589 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
GO:0071973 - bacterial-type flagellum-dependent cell motility Inferred by computational analysis [GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Hauser14, Rajagopala14, Rajagopala09, Marykwas96]
GO:0003774 - motor activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0009288 - bacterial-type flagellum Inferred by computational analysis [UniProtGOA11a]
GO:0009425 - bacterial-type flagellum basal body Inferred by computational analysis [UniProtGOA11]
GO:0009431 - bacterial-type flagellum basal body, MS ring Inferred by computational analysis [GOA01a]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
metabolism biosynthesis of macromolecules (cellular constituents) flagellum

Unification Links: DIP:DIP-401N , EcoliWiki:b1938 , PR:PRO_000022657 , Pride:P25798 , Protein Model Portal:P25798 , RefSeq:NP_416448 , String:511145.b1938 , UniProt:P25798

Relationship Links: InterPro:IN-FAMILY:IPR000067 , InterPro:IN-FAMILY:IPR006182 , InterPro:IN-FAMILY:IPR013556 , Pfam:IN-FAMILY:PF01514 , Pfam:IN-FAMILY:PF08345 , Prints:IN-FAMILY:PR01009

Summary:
FliF is the basic subunit that polymerizes to form the MS ring structure complex of the flagellar basal body [Ueno92].

Essentiality data for fliF knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellar Motor Complex: flagellar basal-body protein FliE

Synonyms: Fla, FlaN, FliE

Gene: fliE Accession Numbers: EG11346 (EcoCyc), b1937, ECK1935

Locations: cell projection

Sequence Length: 104 AAs

Molecular Weight: 11.127 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
GO:0071973 - bacterial-type flagellum-dependent cell motility Inferred by computational analysis [GOA01a]
Molecular Function: GO:0003774 - motor activity Inferred by computational analysis [GOA01a]
GO:0005198 - structural molecule activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0009288 - bacterial-type flagellum Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0009425 - bacterial-type flagellum basal body Inferred by computational analysis [UniProtGOA11]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
metabolism biosynthesis of macromolecules (cellular constituents) flagellum

Unification Links: EcoliWiki:b1937 , Pride:P0A8T5 , Protein Model Portal:P0A8T5 , RefSeq:NP_416447 , String:511145.b1937 , UniProt:P0A8T5

Relationship Links: InterPro:IN-FAMILY:IPR001624 , Pfam:IN-FAMILY:PF02049 , Prints:IN-FAMILY:PR01006

Summary:
FliE is a component of the basal body assembly. Its stoichiometry is estimated to be about 9 subunits per basal body [SaijoHamano04].

Essentiality data for fliE knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellum: Flagellar Export Apparatus

Summary:
The flagellar export apparatus is a type III secretion system that functions in the export of several components of the flagellum across the cytoplasmic membrane into the channel of the flagellum for assembly. The export apparatus consists of six integral membrane proteins (FliO, FliP, FliQ, FliR, FlhA, and FlhB) and three soluble proteins (FliH, FliI, and FliJ) and interacts with several soluble chaperones (FliS, FliT, and FlgN) and the hook-length control protein (FliK). The flagellar motor switch complex proteins (FliG, FliM, and FliN) also take part in interactions affecting protein export.

The six integral membrane proteins of the flagellar export apparatus are embedded in the membrane within the MS ring of the basal body where the apparatus can deliver substrates across the cytoplasmic membrane to the distal end of the growing flagellum [Minamino04]. It is thought that FliO, FliP, FliQ, FliR, FlhA and FlhB comprise the protein-conducting channel of the flagellar export apparatus [Minamino99]. Binding studies show that the FlhA cytoplasmic region associates with FliH, FliI and FliJ as well as with the cytoplasmic domain of FlhB and flagellar export substrates, and that the cytoplasmic region of FlhB associates with FliH, FliI, and FliJ [Minamino00a, Zhu02]. The transmembrane region of FlhA interacts with the MS ring [Kihara01a]. FlhA has also been shown to interact with FliO, FliP, and FliQ [McMurry04].

FliI is a cytoplasmic component of the export apparatus and serves as the ATPase, providing the energy for translocation of export substrates across the cytoplasmic membrane [Fan96]. FliI exists as a monomer in solution [Minamino00b] but is capable of forming a heterotrimeric complex with a dimer of the cytoplasmic protein FliH, the FliI inhibitor. FliH inhibits FliI ATPase activity to conserve energy until protein export can occur by preventing premature oligomerization of FliI [Minamino06]. FliH also acts in targeting of FliI to the export apparatus by binding the FliN protein of the motor switch complex [McMurry06]. In its active form, in the presence of ATP, FliI undergoes oligomerization, forming a hexameric ring structure that binding studies have indicated associates with the cytoplasmic domains of FlhB and FlhA [Minamino00a, Zhu02]. The ATPase activity of FliI has been shown to be cooperative, suggesting that the oligomerization of FliI plays a physiologically significant role [Claret03]. It is unclear whether FliH dissociates from the complex when FliI attaches to the export apparatus [Minamino06]. Binding studies also indicate FliH interacts with FlhA and FlhB [Minamino00a, Zhu02], as well as FliJ [GonzalezPedrajo02]. FliH is not essential for flagellar protein export [Minamino03]. FliJ has been shown to suppress self-aggregation of several flagellar export substrates [Minamino00c]. Mutation studies showed that FliJ is a general component of the flagellar export apparatus that displays chaperone-like activity for both rod/hook-type and filament-type export substrates [Minamino00d]. Binding studies indicate FliJ interacts with both FliH and FlhA [GonzalezPedrajo02, Fraser03], as well as FliM, though the presence of FliJ weakens FliM/FliN and FliN/FliH interactions [GonzalezPedrajo06].

The proteins of the flagellar motor switch complex are also involved in flagellar assembly because null mutations are non-flagellate. FliN is responsible for binding of substrate-bound cytosolic components of the flagellar export apparatus to direct them to the membrane components for export of the substrate. Co-purification studies reveal complexes of FliG, FliM, FliN, FliH, and FliI [GonzalezPedrajo06]. FliN was shown to bind FliH in a manner that does not disrupt the FliM/FliN and FliH/FliI interactions.

In order to make assembly of the flagellum more efficient, proteins required early in the assembly process, such as hook and rod proteins, are transported before proteins of more distal structures. There are two main specificity classes of exported proteins: the rod/hook type and the filament type. The initial state of the export apparatus involves export of rod/hook type substrates, which include FliE, FlgB, FlgC, FlgD, FlgE, FlgF, FlgG, FlgJ, and FliK. FlhB, along with hook-length control protein FliK, coordinates the switching in export specificity from rod/hook-type proteins to filament-type proteins [Kubori00]. FliK is the sensor and transmitter of the hook completion signal [Minamino04a]. An "infrequent ruler function model" suggest the N-terminal domain of FliK, which binds both FlgE and FlgD proteins, acts as a molecular ruler to determine when the hook has reached the appropriate length [Moriya06, Minamino06a]. The model also suggests that the timing of the hook completion signal is determined when a FliK protein happens to be transported at a time when the hook is of approximately the correct length [Moriya06, Minamino06a]. This is supported by the fact that FliK has no apparent function within the periplasm [Hirano05]. Upon completion of the flagellar hook structure, the C-terminal domain of FliK is able to communicate directly with the C-terminal cytoplasmic domain FlhB [Minamino00c, Minamino04a], which undergoes autocatalytic cleavage producing FlhB(CN) and FlhB(CC), which remain tightly associated [Ferris05]. This results in switching of export substrate specificity from rod/hook-type proteins to filament-type proteins, which include FlgK, FlgL, FlgM, FliC, and FliD [Minamino04].

FlgN acts as a chaperone for FlgK and FlgL. FliS and FliT act as a chaperones for FliC and FliD, respectively. Mutation studies show that the FlgNK, FlgNL, FliSC, and FliTD substrate-chaperone complexes dock at FliI for export of the substrates [Thomas04].


Subunit of Flagellar Export Apparatus: flagellar biosynthesis protein FlhA

Synonyms: FlaH, FlhA

Gene: flhA Accession Numbers: G370 (EcoCyc), b1879, ECK1880

Locations: inner membrane

Sequence Length: 692 AAs

Molecular Weight: 74.843 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0044780 - bacterial-type flagellum assembly Inferred from experiment Inferred by computational analysis [GOA01a, Suzuki81]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0009306 - protein secretion Inferred by computational analysis [GOA01a]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11a]
GO:0044781 - bacterial-type flagellum organization Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Daley05]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
cell structure membrane
metabolism biosynthesis of macromolecules (cellular constituents) flagellum

Unification Links: EcoliWiki:b1879 , PR:PRO_000022650 , Pride:P76298 , Protein Model Portal:P76298 , RefSeq:NP_416393 , SMR:P76298 , String:511145.b1879 , UniProt:P76298

Relationship Links: InterPro:IN-FAMILY:IPR001712 , InterPro:IN-FAMILY:IPR006301 , InterPro:IN-FAMILY:IPR025505 , Pfam:IN-FAMILY:PF00771 , Prints:IN-FAMILY:PR00949 , Prosite:IN-FAMILY:PS00994

Summary:
FlhA is one of six integral membrane components of the flagellar export apparatus. FlhA has two regions: the hydrophobic N-terminal transmembrane region with eight membrane-spanning segments and the C-terminal cytoplasmic domain [Kutsukake94]. The structures of the C-terminal domain of FlhA and a fragment of the domain have been determined by X-ray crystallography to a resolution of 2.9 and 3.2 Å, respectively [SaijoHamano05]. Temperature-sensitive mutations in the cytoplasmic region of FlhA can prevent flagellar export [Minamino00a].

FlhA is osmosensitive and is involved in the stress response at pH 6.5 or lower [Trchounian13].

Essentiality data for flhA knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellar Export Apparatus: flagellar biosynthesis protein FlhB

Synonyms: YecQ, FlaG, FlhB

Gene: flhB Accession Numbers: G7028 (EcoCyc), b1880, ECK1881

Locations: inner membrane

Sequence Length: 382 AAs

Molecular Weight: 42.238 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0009306 - protein secretion Inferred by computational analysis [GOA01a]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0044780 - bacterial-type flagellum assembly Inferred by computational analysis [GOA01a]
GO:0044781 - bacterial-type flagellum organization Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Daley05]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]

MultiFun Terms: cell structure flagella
cell structure membrane

Unification Links: EcoliWiki:b1880 , PR:PRO_000022651 , Pride:P76299 , Protein Model Portal:P76299 , RefSeq:NP_416394 , SMR:P76299 , String:511145.b1880 , UniProt:P76299

Relationship Links: InterPro:IN-FAMILY:IPR006135 , InterPro:IN-FAMILY:IPR006136 , Pfam:IN-FAMILY:PF01312 , Prints:IN-FAMILY:PR00950

Summary:
FlhB is one of six integral membrane components of the flagellar export apparatus. FlhB has two regions: the hydrophobic N-terminal domain which, according to hydophobicity studies, crosses the cytoplasmic membrane four times and the C-terminal cytoplasmic domain [Kutsukake94].

Essentiality data for flhB knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellar Export Apparatus: flagellar biosynthesis protein FliO

Synonyms: FlbD, FliO

Gene: fliO Accession Numbers: EG11224 (EcoCyc), b1947, ECK1945

Locations: inner membrane, cell projection

Sequence Length: 121 AAs

Molecular Weight: 12.67 kD (from nucleotide sequence)

Molecular Weight: 13 kD (experimental) [Malakooti94]

GO Terms:

Biological Process: GO:0006935 - chemotaxis Inferred by computational analysis [UniProtGOA11a]
GO:0044781 - bacterial-type flagellum organization Inferred by computational analysis [GOA01a]
GO:0097588 - archaeal or bacterial-type flagellum-dependent cell motility Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09]
GO:0009288 - bacterial-type flagellum Inferred by computational analysis [UniProtGOA11a]
GO:0009425 - bacterial-type flagellum basal body Inferred by computational analysis [UniProtGOA11]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
metabolism biosynthesis of macromolecules (cellular constituents) flagellum

Unification Links: EcoliWiki:b1947 , Pride:P22586 , Protein Model Portal:P22586 , RefSeq:NP_416457 , String:511145.b1947 , UniProt:P22586

Relationship Links: InterPro:IN-FAMILY:IPR022781 , Pfam:IN-FAMILY:PF04347

Summary:
FliO is one of six integral membrane components of the flagellar export apparatus [Minamino04]. FliO has a small N-terminal cytoplasmic domain, a hydrophobic domain consisting of a single transmembrane helix and a considerable periplasmic domain [Minamino99].

Essentiality data for fliO knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellar Export Apparatus: flagellar biosynthesis protein FliP

Synonyms: FlaR, FliP

Gene: fliP Accession Numbers: EG11975 (EcoCyc), b1948, ECK1946

Locations: inner membrane, cell projection

Sequence Length: 245 AAs

Molecular Weight: 26.928 kD (from nucleotide sequence)

Molecular Weight: 25 kD (experimental) [Malakooti94]

GO Terms:

Biological Process: GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0009306 - protein secretion Inferred by computational analysis [GOA01a]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11a]
GO:0044781 - bacterial-type flagellum organization Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Zhang07, Daley05]
GO:0009425 - bacterial-type flagellum basal body Inferred by computational analysis [UniProtGOA11]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
metabolism biosynthesis of macromolecules (cellular constituents) flagellum

Unification Links: EcoliWiki:b1948 , PR:PRO_000022666 , Protein Model Portal:P0AC05 , RefSeq:NP_416458 , String:511145.b1948 , UniProt:P0AC05

Relationship Links: InterPro:IN-FAMILY:IPR005837 , InterPro:IN-FAMILY:IPR005838 , Pfam:IN-FAMILY:PF00813 , Prints:IN-FAMILY:PR00951 , Prints:IN-FAMILY:PR01302 , Prosite:IN-FAMILY:PS01060 , Prosite:IN-FAMILY:PS01061

Summary:
FliP is one of six integral membrane components of the flagellar export apparatus [Minamino04, Fan97]. FliP has a substantial periplasmic domain between two of its four transmembrane domains [Minamino99].

Essentiality data for fliP knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellar Export Apparatus: flagellar biosynthesis protein FliQ

Synonyms: FlaQ, FliQ

Gene: fliQ Accession Numbers: EG11976 (EcoCyc), b1949, ECK1947

Locations: inner membrane, cell projection

Sequence Length: 89 AAs

Molecular Weight: 9.632 kD (from nucleotide sequence)

Molecular Weight: 10 kD (experimental) [Malakooti94]

GO Terms:

Biological Process: GO:0009306 - protein secretion Inferred by computational analysis [GOA01a]
GO:0044780 - bacterial-type flagellum assembly Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09]
GO:0009288 - bacterial-type flagellum Inferred by computational analysis [UniProtGOA11a]
GO:0009425 - bacterial-type flagellum basal body Inferred by computational analysis [UniProtGOA11]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]

MultiFun Terms: cell structure flagella
metabolism biosynthesis of macromolecules (cellular constituents) flagellum
metabolism biosynthesis of macromolecules (cellular constituents) glycoprotein

Unification Links: EcoliWiki:b1949 , Protein Model Portal:P0AC07 , RefSeq:NP_416459 , String:511145.b1949 , UniProt:P0AC07

Relationship Links: InterPro:IN-FAMILY:IPR002191 , InterPro:IN-FAMILY:IPR006305 , Pfam:IN-FAMILY:PF01313 , Prints:IN-FAMILY:PR00952

Summary:
FliQ is one of six integral membrane components of the flagellar export apparatus [Minamino04]. FliQ has two transmembrane domains [Minamino99].

Essentiality data for fliQ knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellar Export Apparatus: flagellar biosynthesis protein FliR

Synonyms: FlaP, FliR

Gene: fliR Accession Numbers: EG11977 (EcoCyc), b1950, ECK1948

Locations: inner membrane, cell projection

Sequence Length: 261 AAs

Molecular Weight: 28.543 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006605 - protein targeting Inferred by computational analysis [GOA01a]
GO:0044780 - bacterial-type flagellum assembly Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Daley05]
GO:0009288 - bacterial-type flagellum Inferred by computational analysis [UniProtGOA11a]
GO:0009425 - bacterial-type flagellum basal body Inferred by computational analysis [UniProtGOA11]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]

MultiFun Terms: cell structure flagella
transport Putative uncharacterized transport protein

Unification Links: EcoliWiki:b1950 , PR:PRO_000022667 , Protein Model Portal:P33135 , RefSeq:NP_416460 , String:511145.b1950 , UniProt:P33135

Relationship Links: InterPro:IN-FAMILY:IPR002010 , InterPro:IN-FAMILY:IPR006303 , Pfam:IN-FAMILY:PF01311 , Prints:IN-FAMILY:PR00953

Summary:
FliR is one of six integral membrane components of the flagellar export apparatus [Minamino04, Fan97]. FliR has five or six transmembrane helices connected by short loops [Ohnishi97].

Essentiality data for fliR knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellar Export Apparatus: flagellar biosynthesis protein FliH

Synonyms: FliH

Gene: fliH Accession Numbers: EG11656 (EcoCyc), b1940, ECK1938

Locations: cytosol, cell projection

Sequence Length: 228 AAs

Molecular Weight: 25.05 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11a]
GO:0044781 - bacterial-type flagellum organization Inferred by computational analysis [UniProtGOA11a]
GO:0071973 - bacterial-type flagellum-dependent cell motility Inferred by computational analysis [GOA01a]
Molecular Function: GO:0003774 - motor activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, LopezCampistrou05]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0009288 - bacterial-type flagellum Inferred by computational analysis [GOA01a]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
metabolism biosynthesis of macromolecules (cellular constituents) flagellum

Unification Links: DIP:DIP-9654N , EcoliWiki:b1940 , PR:PRO_000022659 , Protein Model Portal:P31068 , RefSeq:NP_416450 , String:511145.b1940 , UniProt:P31068

Relationship Links: InterPro:IN-FAMILY:IPR000563 , InterPro:IN-FAMILY:IPR018035 , Pfam:IN-FAMILY:PF02108 , Prints:IN-FAMILY:PR01003

Summary:
FliH is a cytoplasmic protein which exists as a dimer in solution and forms a stable heterotrimeric complex with FliI, inhibiting its ATPase activity [Minamino00b].

Essentiality data for fliH knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellar Export Apparatus: flagellum-specific ATP synthase FliI

Synonyms: Fla, FlaC, FliI

Gene: fliI Accession Numbers: G377 (EcoCyc), b1941, ECK1939

Locations: inner membrane, cytosol

Sequence Length: 457 AAs

Molecular Weight: 49.316 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006200 - ATP catabolic process Inferred by computational analysis [GOA01a]
GO:0006754 - ATP biosynthetic process Inferred by computational analysis [UniProtGOA11a]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11a]
GO:0009058 - biosynthetic process Inferred by computational analysis [GOA01a]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11a]
GO:0015992 - proton transport Inferred by computational analysis [UniProtGOA11a]
GO:0030254 - protein secretion by the type III secretion system Inferred by computational analysis [GOA01a]
GO:0044780 - bacterial-type flagellum assembly Inferred by computational analysis [GOA01a]
GO:0044781 - bacterial-type flagellum organization Inferred by computational analysis [UniProtGOA11a]
GO:0071973 - bacterial-type flagellum-dependent cell motility Inferred by computational analysis [GOA01a]
Molecular Function: GO:0042802 - identical protein binding Inferred from experiment [Marykwas96, Rajagopala14, Rajagopala09]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016887 - ATPase activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA01a]
GO:0005886 - plasma membrane Inferred by computational analysis [DiazMejia09]
GO:0030257 - type III protein secretion system complex Inferred by computational analysis [GOA01a]

MultiFun Terms: cell structure flagella
metabolism energy metabolism, carbon ATP proton motive force interconversion

Unification Links: DIP:DIP-9655N , EcoliWiki:b1941 , ModBase:P52612 , PR:PRO_000022660 , Pride:P52612 , Protein Model Portal:P52612 , RefSeq:NP_416451 , SMR:P52612 , String:511145.b1941 , UniProt:P52612

Relationship Links: InterPro:IN-FAMILY:IPR000194 , InterPro:IN-FAMILY:IPR003593 , InterPro:IN-FAMILY:IPR005714 , InterPro:IN-FAMILY:IPR020003 , InterPro:IN-FAMILY:IPR020005 , InterPro:IN-FAMILY:IPR027417 , Panther:IN-FAMILY:PTHR15184:SF9 , Pfam:IN-FAMILY:PF00006 , Prosite:IN-FAMILY:PS00152 , Smart:IN-FAMILY:SM00382

Summary:
FliI is a cytoplasmic component of the flagellar export apparatus and serves as the ATPase of the apparatus, providing the energy for translocation of export substrates across the cytoplasmic membrane [Fan96]. The structure of FliI missing the N-terminal 18 amino acids was determined by X-ray crystallography to a resolution of 2.4 Å [Minamino06b].

Essentiality data for fliI knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellar Export Apparatus: flagellar biosynthesis protein FliJ

Synonyms: FlaO, FliJ

Gene: fliJ Accession Numbers: G378 (EcoCyc), b1942, ECK1940

Locations: inner membrane, cell projection

Sequence Length: 147 AAs

Molecular Weight: 17.307 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0006935 - chemotaxis Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11a]
GO:0044781 - bacterial-type flagellum organization Inferred by computational analysis [UniProtGOA11a]
GO:0071973 - bacterial-type flagellum-dependent cell motility Inferred by computational analysis [GOA01a]
Molecular Function: GO:0003774 - motor activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0009288 - bacterial-type flagellum Inferred by computational analysis [GOA01a]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
metabolism biosynthesis of macromolecules (cellular constituents) flagellum

Unification Links: DIP:DIP-9656N , EcoliWiki:b1942 , Mint:MINT-1258288 , PR:PRO_000022661 , Pride:P52613 , Protein Model Portal:P52613 , RefSeq:NP_416452 , SMR:P52613 , String:511145.b1942 , UniProt:P52613

Relationship Links: InterPro:IN-FAMILY:IPR012823 , InterPro:IN-FAMILY:IPR018006 , Pfam:IN-FAMILY:PF02050 , Prints:IN-FAMILY:PR01004

Summary:
FliJ is one of three soluble components of the flagellar export system, along with FliH and FliI [Minamino99]. FliJ has several feature similarities with the type III cytoplasmic chaperone family [Minamino04].

Essentiality data for fliJ knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellum: flagellar hook protein FlgE

Synonyms: FlaK, FlgE

Gene: flgE Accession Numbers: G361 (EcoCyc), b1076, ECK1061

Locations: cytosol, cell projection

Sequence Length: 402 AAs

Molecular Weight: 42.045 kD (from nucleotide sequence)

Molecular Weight: 42 kD (experimental) [Komeda78]

GO Terms:

Biological Process: GO:0071973 - bacterial-type flagellum-dependent cell motility Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment [LopezCampistrou05]
GO:0009424 - bacterial-type flagellum hook Inferred from experiment [Komeda84, Komeda78a]
GO:0009288 - bacterial-type flagellum Inferred by computational analysis [UniProtGOA11a]
GO:0009425 - bacterial-type flagellum basal body Inferred by computational analysis [UniProtGOA11]
GO:0030694 - bacterial-type flagellum basal body, rod Inferred by computational analysis [GOA01a]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
metabolism biosynthesis of macromolecules (cellular constituents) flagellum

Unification Links: EcoliWiki:b1076 , PR:PRO_000022641 , Pride:P75937 , Protein Model Portal:P75937 , RefSeq:NP_415594 , SMR:P75937 , String:511145.b1076 , Swiss-Model:P75937 , UniProt:P75937

Relationship Links: InterPro:IN-FAMILY:IPR001444 , InterPro:IN-FAMILY:IPR010930 , InterPro:IN-FAMILY:IPR011491 , InterPro:IN-FAMILY:IPR019776 , InterPro:IN-FAMILY:IPR020013 , Pfam:IN-FAMILY:PF00460 , Pfam:IN-FAMILY:PF06429 , Pfam:IN-FAMILY:PF07559 , Prosite:IN-FAMILY:PS00588

Summary:
FlgE is the basic subunit that polymerizes to form the flexible hook structure which couples the envelope-embedded flagellar rotary motor to the rigid flagellar filament in Escherichia coli.

Essentiality data for flgE knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellum: flagellar biosynthesis, hook-filament junction protein 1

Synonyms: FlaS, FlgK

Gene: flgK Accession Numbers: EG11967 (EcoCyc), b1082, ECK1067

Locations: extracellular space, cell projection

Sequence Length: 547 AAs

Molecular Weight: 57.93 kD (from nucleotide sequence)

Molecular Weight: 60 kD (experimental) [Komeda78]

GO Terms:

Biological Process: GO:0044780 - bacterial-type flagellum assembly Inferred from experiment Inferred by computational analysis [GOA01a, Suzuki81]
GO:0071973 - bacterial-type flagellum-dependent cell motility Inferred by computational analysis [GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Rajagopala09, Arifuzzaman06]
GO:0005198 - structural molecule activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005576 - extracellular region Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0009288 - bacterial-type flagellum Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0009424 - bacterial-type flagellum hook Inferred by computational analysis [GOA01a]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
information transfer protein related chaperoning, repair (refolding)
metabolism biosynthesis of macromolecules (cellular constituents) flagellum

Unification Links: DIP:DIP-9639N , EcoliWiki:b1082 , Mint:MINT-1322777 , PR:PRO_000022646 , Pride:P33235 , Protein Model Portal:P33235 , RefSeq:NP_415600 , SMR:P33235 , String:511145.b1082 , UniProt:P33235

Relationship Links: InterPro:IN-FAMILY:IPR001444 , InterPro:IN-FAMILY:IPR002371 , InterPro:IN-FAMILY:IPR010930 , Pfam:IN-FAMILY:PF00460 , Pfam:IN-FAMILY:PF06429 , Prints:IN-FAMILY:PR01005 , Prosite:IN-FAMILY:PS00588

Summary:
Experiments in Salmonella typhimurium using antibodies against the flagellar proteins FlgK and FlgL identify them as junction proteins which connect the filament to the hook [Ikeda87].

Essentiality data for flgK knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellum: flagellar biosynthesis; hook-filament junction protein

Synonyms: FlaT, FlgL

Gene: flgL Accession Numbers: EG11545 (EcoCyc), b1083, ECK1068

Locations: extracellular space, cell projection

Sequence Length: 317 AAs

Molecular Weight: 34.281 kD (from nucleotide sequence)

Molecular Weight: 35 kD (experimental) [Komeda78]

GO Terms:

Biological Process: GO:0071973 - bacterial-type flagellum-dependent cell motility Inferred by computational analysis [GOA01a]
Molecular Function: GO:0005198 - structural molecule activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005576 - extracellular region Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0009288 - bacterial-type flagellum Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA01a]
GO:0009424 - bacterial-type flagellum hook Inferred by computational analysis [GOA01a]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
information transfer protein related chaperoning, repair (refolding)
metabolism biosynthesis of macromolecules (cellular constituents) flagellum

Unification Links: EcoliWiki:b1083 , ModBase:P29744 , PR:PRO_000022647 , Pride:P29744 , Protein Model Portal:P29744 , RefSeq:NP_415601 , SMR:P29744 , String:511145.b1083 , UniProt:P29744

Relationship Links: InterPro:IN-FAMILY:IPR001029 , InterPro:IN-FAMILY:IPR013384 , Pfam:IN-FAMILY:PF00669

Summary:
Experiments in Salmonella typhimurium using antibodies against the flagellar proteins FlgK and FlgL identify them as junction proteins which connect the filament to the hook [Ikeda87].

Essentiality data for flgL knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellum: flagellar biosynthesis; flagellin, filament structural protein

Synonyms: Hag, FlaF, FliC

Gene: fliC Accession Numbers: EG10321 (EcoCyc), b1923, ECK1922

Locations: extracellular space, cell projection

Sequence Length: 498 AAs

Molecular Weight: 51.295 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0071973 - bacterial-type flagellum-dependent cell motility Inferred by computational analysis [GOA01a]
Molecular Function: GO:0005198 - structural molecule activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005576 - extracellular region Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0009288 - bacterial-type flagellum Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA01a]
GO:0009420 - bacterial-type flagellum filament Inferred by computational analysis [GOA01a]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
metabolism biosynthesis of macromolecules (cellular constituents) flagellum

Unification Links: DIP:DIP-9649N , EcoliWiki:b1923 , ModBase:P04949 , PR:PRO_000022655 , Pride:P04949 , Protein Model Portal:P04949 , RefSeq:NP_416433 , SMR:P04949 , String:511145.b1923 , UniProt:P04949

Relationship Links: InterPro:IN-FAMILY:IPR001029 , InterPro:IN-FAMILY:IPR001492 , InterPro:IN-FAMILY:IPR014981 , Pfam:IN-FAMILY:PF00669 , Pfam:IN-FAMILY:PF00700 , Pfam:IN-FAMILY:PF08884 , Prints:IN-FAMILY:PR00207

Summary:
FliC, or flagellin, is the basic subunit that polymerizes to form the rigid flagellar filament of Escherichia coli.

Essentiality data for fliC knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Subunit of Flagellum: flagellar cap protein FliD; filament capping protein; enables filament assembly

Synonyms: Rfs, FlbC, FliD

Gene: fliD Accession Numbers: EG10841 (EcoCyc), b1924, ECK1923

Locations: extracellular space, cell projection

Sequence Length: 468 AAs

Molecular Weight: 48.456 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0007155 - cell adhesion Inferred by computational analysis [GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Rajagopala09]
Cellular Component: GO:0005576 - extracellular region Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0009288 - bacterial-type flagellum Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA01a]
GO:0009424 - bacterial-type flagellum hook Inferred by computational analysis [GOA01a]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
metabolism biosynthesis of macromolecules (cellular constituents) flagellum

Unification Links: EcoliWiki:b1924 , PR:PRO_000022656 , Pride:P24216 , Protein Model Portal:P24216 , RefSeq:NP_416434 , String:511145.b1924 , UniProt:P24216

Relationship Links: InterPro:IN-FAMILY:IPR003481 , InterPro:IN-FAMILY:IPR010809 , Pfam:IN-FAMILY:PF02465 , Pfam:IN-FAMILY:PF07195

Summary:
The filament cap lies at the distal, growing end of the flagellar filament and plays a critical role in the assembly of flagellin (FliC) monomers into the growing filament [Homma84].

Essentiality data for fliD knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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