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Escherichia coli K-12 substr. MG1655 Polypeptide: essential cell division protein FtsB

Gene: ftsB Accession Numbers: G7424 (EcoCyc), b2748, ECK2743

Synonyms: ygbQ

Regulation Summary Diagram: ?

Regulation summary diagram for ftsB

Component of: FtsLBQ cell division complex (summary available)

FtsB is an essential cell division protein which localizes to the cell division site. Depletion of FtsB results in abnormal filamentous morphology, but does not cause a defect in segregation of replicated DNA [Buddelmeijer02].

Localization of FtsB to the division site is dependent on FtsQ and FtsL, but does not require FtsW and FtsI. Conversely, FtsB is required for localization of FtsI and FtsW to the Z ring [Buddelmeijer02]. Although the hierarchy of dependency in the assembly of cell division proteins is largely linear, recent results showed that assembly of the cell division machinery is complex. Premature targeting of FtsB to the division site enables recruitment of FtsL, FtsW and FtsI in the absence of FtsQ [Goehring06].

FtsB contains a small N-terminal cytoplasmic domain, a membrane-spanning region and a periplasmic C-terminal domain with a leucine zipper motif [Buddelmeijer02]. The transmembrane domain homo-oligomerizes; the interaction is mediated by and polar amino acids on one face of the helix and hydrogen bonding of Gln16 [LaPointe13]. A crystal structure of the periplasmic domain has been solved, showing a canonical coiled-coil structure [LaPointe13].

FtsB and FtsL localization to the constriction site is codependent [Buddelmeijer02]; the periplasmic leucine zipper motif is required for optimal interaction between FtsL and FtsB [Robichon11]. FtsQ, FtsL and FtsB form a complex in vivo even in the absence of FtsK and thus independently of their localization to the septal region [Buddelmeijer04]. The N-terminal half of FtsB including parts of the periplasmic coiled-coil domain is required for its interaction with FtsL; in the complex with FtsL, this region is also sufficient for recruitment of downstream division proteins [Gonzalez09]. The transmembrane helices of FtsB and FtsL appear to be major contributors to the stability of a 1:1 higher-order oligomeric complex between FtsB and FtsL [Khadria13]. A part of the periplasmic C-terminal domain is required for interaction with FtsQ [Gonzalez09].

Overexpression of ftsB can partially suppress the viability and cell division phenotypes of an ftsK mutant [Geissler05].

Selected reviews: [deBoer10, Weiss04, Errington03]

Locations: inner membrane

Map Position: [2,870,531 <- 2,870,842] (61.87 centisomes, 223°)
Length: 312 bp / 103 aa

Molecular Weight of Polypeptide: 11.622 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0009019 , DIP:DIP-12117N , EchoBASE:EB2914 , EcoGene:EG13111 , EcoliWiki:b2748 , OU-Microarray:b2748 , PortEco:ftsB , PR:PRO_000022715 , Pride:P0A6S5 , Protein Model Portal:P0A6S5 , RefSeq:NP_417228 , RegulonDB:G7424 , SMR:P0A6S5 , String:511145.b2748 , UniProt:P0A6S5

Relationship Links: InterPro:IN-FAMILY:IPR007060 , InterPro:IN-FAMILY:IPR023081 , PDB:Structure:4IFF , Pfam:IN-FAMILY:PF04977

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0043093 - FtsZ-dependent cytokinesis Inferred from experiment Inferred by computational analysis [GOA06, Buddelmeijer02]
GO:0051301 - cell division Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Ricard73, Buddelmeijer02]
GO:0007049 - cell cycle Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Robichon11, Gonzalez10, Gonzalez09, Scheffers07, DUlisse07, Karimova05, Buddelmeijer04]
GO:0042802 - identical protein binding Inferred from experiment [LaPointe13]
Cellular Component: GO:0030428 - cell septum Inferred from experiment [Buddelmeijer02]
GO:0032155 - cell division site part Inferred from experiment [Buddelmeijer02]
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0005887 - integral component of plasma membrane Inferred by computational analysis [GOA06]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]
GO:0032153 - cell division site Inferred by computational analysis [GOA06]

MultiFun Terms: cell processes cell division

Essentiality data for ftsB knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Last-Curated ? 20-Feb-2014 by Keseler I , SRI International

Subunit of: FtsLBQ cell division complex

Subunit composition of FtsLBQ cell division complex = [FtsQ][FtsB][FtsL]
         essential cell division protein FtsQ = FtsQ (extended summary available)
         essential cell division protein FtsB = FtsB (extended summary available)
         essential cell division protein FtsL = FtsL (extended summary available)

The FtsL, FtsB and FtsQ cell division proteins form a complex independently of its location at the cell division site [Buddelmeijer04]. This complex is thought to function as a molecular scaffold that enables proper formation of the divisome.

A structural model of the periplasmic component of the FtsLBQ complex has been generated, indicating a trimeric or hexameric coiled-coil structure [Villanelo11]. A current hypothesis is that a dimer of FtsB recruits FtsL into a higher-order complex with 1:1 stoichiometry [Khadria13].

Created 21-Jun-2011 by Keseler I , SRI International

Sequence Features

Protein sequence of essential cell division protein FtsB with features indicated

Feature Class Location Citations Comment
Transmembrane-Region 4 -> 21
UniProt: Helical;; Non-Experimental Qualifier: potential;
Protein-Segment 41 -> 72
UniProt: Leucine zipper-like; Sequence Annotation Type: short sequence motif.

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


Peter D. Karp on Thu Jan 16, 2003:
Predicted gene function revised as a result of E. coli genome reannotation by Serres et al. [Serres01 ].
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


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

Buddelmeijer02: Buddelmeijer N, Judson N, Boyd D, Mekalanos JJ, Beckwith J (2002). "YgbQ, a cell division protein in Escherichia coli and Vibrio cholerae, localizes in codependent fashion with FtsL to the division site." Proc Natl Acad Sci U S A 2002;99(9);6316-21. PMID: 11972052

Buddelmeijer04: Buddelmeijer N, Beckwith J (2004). "A complex of the Escherichia coli cell division proteins FtsL, FtsB and FtsQ forms independently of its localization to the septal region." Mol Microbiol 52(5);1315-27. PMID: 15165235

deBoer10: de Boer PA (2010). "Advances in understanding E. coli cell fission." Curr Opin Microbiol 13(6);730-7. PMID: 20943430

DUlisse07: D'Ulisse V, Fagioli M, Ghelardini P, Paolozzi L (2007). "Three functional subdomains of the Escherichia coli FtsQ protein are involved in its interaction with the other division proteins." Microbiology 153(Pt 1);124-38. PMID: 17185541

Errington03: Errington J, Daniel RA, Scheffers DJ (2003). "Cytokinesis in bacteria." Microbiol Mol Biol Rev 67(1);52-65. PMID: 12626683

Geissler05: Geissler B, Margolin W (2005). "Evidence for functional overlap among multiple bacterial cell division proteins: compensating for the loss of FtsK." Mol Microbiol 58(2);596-612. PMID: 16194242

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Goehring06: Goehring NW, Gonzalez MD, Beckwith J (2006). "Premature targeting of cell division proteins to midcell reveals hierarchies of protein interactions involved in divisome assembly." Mol Microbiol 61(1);33-45. PMID: 16824093

Gonzalez09: Gonzalez MD, Beckwith J (2009). "Divisome under construction: distinct domains of the small membrane protein FtsB are necessary for interaction with multiple cell division proteins." J Bacteriol 191(8);2815-25. PMID: 19233928

Gonzalez10: Gonzalez MD, Akbay EA, Boyd D, Beckwith J (2010). "Multiple interaction domains in FtsL, a protein component of the widely conserved bacterial FtsLBQ cell division complex." J Bacteriol 192(11);2757-68. PMID: 20363951

Karimova05: Karimova G, Dautin N, Ladant D (2005). "Interaction network among Escherichia coli membrane proteins involved in cell division as revealed by bacterial two-hybrid analysis." J Bacteriol 187(7);2233-43. PMID: 15774864

Khadria13: Khadria AS, Senes A (2013). "The transmembrane domains of the bacterial cell division proteins FtsB and FtsL form a stable high-order oligomer." Biochemistry 52(43);7542-50. PMID: 24083359

LaPointe13: LaPointe LM, Taylor KC, Subramaniam S, Khadria A, Rayment I, Senes A (2013). "Structural organization of FtsB, a transmembrane protein of the bacterial divisome." Biochemistry 52(15);2574-85. PMID: 23520975

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

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

Robichon11: Robichon C, Karimova G, Beckwith J, Ladant D (2011). "Role of leucine zipper motifs in association of the Escherichia coli cell division proteins FtsL and FtsB." J Bacteriol 193(18);4988-92. PMID: 21784946

Scheffers07: Scheffers DJ, Robichon C, Haan GJ, den Blaauwen T, Koningstein G, van Bloois E, Beckwith J, Luirink J (2007). "Contribution of the FtsQ transmembrane segment to localization to the cell division site." J Bacteriol 189(20);7273-80. PMID: 17693520

Serres01: Serres MH, Gopal S, Nahum LA, Liang P, Gaasterland T, Riley M (2001). "A functional update of the Escherichia coli K-12 genome." Genome Biol 2(9);RESEARCH0035. PMID: 11574054

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Villanelo11: Villanelo F, Ordenes A, Brunet J, Lagos R, Monasterio O (2011). "A model for the Escherichia coli FtsB/FtsL/FtsQ cell division complex." BMC Struct Biol 11(1);28. PMID: 21672257

Weiss04: Weiss DS (2004). "Bacterial cell division and the septal ring." Mol Microbiol 54(3);588-97. PMID: 15491352

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Thu Sep 3, 2015, biocyc12.