|Gene:||ftsE||Accession Numbers: EG10340 (EcoCyc), b3463, ECK3447|
Component of: protein complex, putative transporter, ABC superfamily (summary available)
FtsE is the putative ATP-binding protein component of an ATP-binding cassette (ABC) transporter. FtsE dimerizes and associates with the inner membrane via interaction with FtsX, an integral membrane protein [deLeeuw99].
FtsE and FtsX localize to the cell division site; localization is dependent on FtsZ, FtsA and ZipA, but not FtsK, FtsQ, FtsL and FtsI [Schmidt04a]. FtsEX is important for assembly or stability of the septal ring under low-salt growth conditions [Schmidt04a].
An ftsE null mutant is only viable on high salt medium [deLeeuw99]. ftsE and ftsX are located in an operon with the ftsY gene. ftsY encodes a GTPase which acts as a receptor for the SRP (signal recognition particle) involved in protein targeting [Gill87, Miller94a]. It has been suggested that FtsE and FtsX are not to be required for SRP-mediated targeting [deLeeuw99], although it has been reported that ftsE mutants are affected in translocation of potassium ion pump proteins into the cytoplasmic membrane [Ukai98].
Locations: inner membrane, cytosol
|Map Position: [3,600,102 <- 3,600,770] (77.59 centisomes, 279°)||Length: 669 bp / 222 aa|
Molecular Weight of Polypeptide: 24.439 kD (from nucleotide sequence)
Unification Links: ASAP:ABE-0011313, CGSC:736, DIP:DIP-47843N, EchoBASE:EB0336, EcoGene:EG10340, EcoliWiki:b3463, Mint:MINT-1233007, ModBase:P0A9R7, OU-Microarray:b3463, PortEco:ftsE, PR:PRO_000022716, Protein Model Portal:P0A9R7, RefSeq:NP_417920, RegulonDB:EG10340, SMR:P0A9R7, String:511145.b3463, UniProt:P0A9R7
Relationship Links: InterPro:IN-FAMILY:IPR003439, InterPro:IN-FAMILY:IPR003593, InterPro:IN-FAMILY:IPR005286, InterPro:IN-FAMILY:IPR017871, InterPro:IN-FAMILY:IPR027417, Panther:IN-FAMILY:PTHR24220:SF186, Pfam:IN-FAMILY:PF00005, Prosite:IN-FAMILY:PS00211, Prosite:IN-FAMILY:PS50893, Smart:IN-FAMILY:SM00382
In Paralogous Gene Group: 23 (75 members)
|MultiFun Terms:||cell processes → cell division|
|transport → Channel-type Transporters → Pyrophosphate Bond (ATP; GTP; P2) Hydrolysis-driven Active Transporters → The ATP-binding Cassette (ABC) Superfamily + ABC-type Uptake Permeases → ABC superfamily ATP binding cytoplasmic component|
|Growth Medium||Growth?||T (°C)||O2||pH||Osm/L||Growth Observations|
|LB Lennox||No||37||Aerobic||7||No [Baba06, Comment 1]|
Subunit composition of
protein complex, putative transporter, ABC superfamily = [FtsE]2[FtsX]
putative transport protein, ABC superfamily - ATP-binding component = FtsE (extended summary available)
putative transport protein, ABC superfamily - membrane component = FtsX (summary available)
FtsE and FtsX are members of the ABC superfamily of transporters [Saurin99]. FtsE is the putative ATP-binding protein and FtsX is the putative membrane component. ftsE and ftsX were originally identified as conditional lethal mutants which failed to septate at the non-permissive temperature, implying a role in cell division [Taschner88]. FtsE and FtsX have been purified and shown to interact by co-immunoprecipitation [deLeeuw99]. The FtsEX complex may function as an ATP-dependent transporter which has a role in cell division and possibly salt transport.
Locations: inner membrane
|Feature Class||Location||Attached Group||Citations||Comment|
|Conserved-Region||2 -> 222|
|Pfam PF00005||18 -> 165|
|Nucleotide-Phosphate-Binding-Region||35 -> 42||ATP|
10/20/97 Gene b3463 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10340; confirmed by SwissProt match.
Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554
Crickmore86: Crickmore N, Salmond GP (1986). "The Escherichia coli heat shock regulatory gene is immediately downstream of a cell division operon: the fam mutation is allelic with rpoH." Mol Gen Genet 205(3);535-9. PMID: 3550388
deLeeuw99: de Leeuw E, Graham B, Phillips GJ, ten Hagen-Jongman CM, Oudega B, Luirink J (1999). "Molecular characterization of Escherichia coli FtsE and FtsX." Mol Microbiol 1999;31(3);983-93. PMID: 10048040
DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114
Finn14: Finn RD, Bateman A, Clements J, Coggill P, Eberhardt RY, Eddy SR, Heger A, Hetherington K, Holm L, Mistry J, Sonnhammer EL, Tate J, Punta M (2014). "Pfam: the protein families database." Nucleic Acids Res 42(Database issue);D222-30. PMID: 24288371
Miller94a: Miller JD, Bernstein HD, Walter P (1994). "Interaction of E. coli Ffh/4.5S ribonucleoprotein and FtsY mimics that of mammalian signal recognition particle and its receptor." Nature 1994;367(6464);657-9. PMID: 8107852
Ricard73: Ricard M, Hirota Y (1973). "Process of cellular division in Escherichia coli: physiological study on thermosensitive mutants defective in cell division." J Bacteriol 116(1);314-22. PMID: 4583216
Saurin99: Saurin W, Hofnung M, Dassa E (1999). "Getting in or out: early segregation between importers and exporters in the evolution of ATP-binding cassette (ABC) transporters." J Mol Evol 1999;48(1);22-41. PMID: 9873074
Schmidt04a: Schmidt KL, Peterson ND, Kustusch RJ, Wissel MC, Graham B, Phillips GJ, Weiss DS (2004). "A predicted ABC transporter, FtsEX, is needed for cell division in Escherichia coli." J Bacteriol 186(3);785-93. PMID: 14729705
Taschner88: Taschner PE, Huls PG, Pas E, Woldringh CL (1988). "Division behavior and shape changes in isogenic ftsZ, ftsQ, ftsA, pbpB, and ftsE cell division mutants of Escherichia coli during temperature shift experiments." J Bacteriol 1988;170(4);1533-40. PMID: 3280547
Ukai98: Ukai H, Matsuzawa H, Ito K, Yamada M, Nishimura A (1998). "ftsE(Ts) affects translocation of K+-pump proteins into the cytoplasmic membrane of Escherichia coli." J Bacteriol 1998;180(14);3663-70. PMID: 9658012
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