FTSB_ECOLI
ID FTSB_ECOLI Reviewed; 103 AA.
AC P0A6S5; Q2MA81; Q46894;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Cell division protein FtsB {ECO:0000255|HAMAP-Rule:MF_00599};
GN Name=ftsB {ECO:0000255|HAMAP-Rule:MF_00599}; Synonyms=ygbQ;
GN OrderedLocusNames=b2748, JW2718;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FTSL, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11972052; DOI=10.1073/pnas.092128499;
RA Buddelmeijer N., Judson N., Boyd D., Mekalanos J.J., Beckwith J.;
RT "YgbQ, a cell division protein in Escherichia coli and Vibrio cholerae,
RT localizes in codependent fashion with FtsL to the division site.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6316-6321(2002).
RN [4]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=15165235; DOI=10.1111/j.1365-2958.2004.04044.x;
RA Buddelmeijer N., Beckwith J.;
RT "A complex of the Escherichia coli cell division proteins FtsL, FtsB and
RT FtsQ forms independently of its localization to the septal region.";
RL Mol. Microbiol. 52:1315-1327(2004).
RN [5]
RP INTERACTION WITH FTSL; FTSQ; FTSI AND FTSN.
RC STRAIN=K12;
RX PubMed=15774864; DOI=10.1128/jb.187.7.2233-2243.2005;
RA Karimova G., Dautin N., Ladant D.;
RT "Interaction network among Escherichia coli membrane proteins involved in
RT cell division as revealed by bacterial two-hybrid analysis.";
RL J. Bacteriol. 187:2233-2243(2005).
RN [6]
RP FUNCTION, SUBUNIT, INTERACTION WITH FTSL AND FTSQ, AND DOMAIN.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=19233928; DOI=10.1128/jb.01597-08;
RA Gonzalez M.D., Beckwith J.;
RT "Divisome under construction: distinct domains of the small membrane
RT protein FtsB are necessary for interaction with multiple cell division
RT proteins.";
RL J. Bacteriol. 191:2815-2825(2009).
RN [7]
RP 3D-STRUCTURE MODELING OF THE FTSB/FTSL/FTSQ COMPLEX.
RX PubMed=21672257; DOI=10.1186/1472-6807-11-28;
RA Villanelo F., Ordenes A., Brunet J., Lagos R., Monasterio O.;
RT "A model for the Escherichia coli FtsB/FtsL/FtsQ cell division complex.";
RL BMC Struct. Biol. 11:28-28(2011).
RN [8]
RP DOMAIN, AND LEUCINE ZIPPER-LIKE MOTIF.
RX PubMed=21784946; DOI=10.1128/jb.00324-11;
RA Robichon C., Karimova G., Beckwith J., Ladant D.;
RT "Role of leucine zipper motifs in association of the Escherichia coli cell
RT division proteins FtsL and FtsB.";
RL J. Bacteriol. 193:4988-4992(2011).
CC -!- FUNCTION: Essential cell division protein. May link together the
CC upstream cell division proteins, which are predominantly cytoplasmic,
CC with the downstream cell division proteins, which are predominantly
CC periplasmic. {ECO:0000255|HAMAP-Rule:MF_00599,
CC ECO:0000269|PubMed:11972052, ECO:0000269|PubMed:19233928}.
CC -!- SUBUNIT: Part of a complex composed of FtsB, FtsL and FtsQ. The complex
CC can be formed before its localization to the division site. This
CC tripartite complex can be divided further into a subcomplex of FtsB and
CC FtsL, which forms in the absence of FtsQ. Interacts also with FtsI and
CC FtsN. {ECO:0000255|HAMAP-Rule:MF_00599, ECO:0000269|PubMed:11972052,
CC ECO:0000269|PubMed:15165235, ECO:0000269|PubMed:15774864,
CC ECO:0000269|PubMed:19233928}.
CC -!- INTERACTION:
CC P0A6S5; P0AEN4: ftsL; NbExp=18; IntAct=EBI-1113953, EBI-1119082;
CC P0A6S5; P06136: ftsQ; NbExp=10; IntAct=EBI-1113953, EBI-1130157;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00599, ECO:0000269|PubMed:11972052,
CC ECO:0000269|PubMed:15165235}; Single-pass type II membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00599, ECO:0000269|PubMed:11972052,
CC ECO:0000269|PubMed:15165235}. Note=Localizes to the division septum.
CC Localization requires FtsQ and FtsL, but not FtsW and FtsI.
CC Localization of FtsB and FtsL is codependent.
CC -!- DOMAIN: The transmembrane segment and the membrane-proximal periplasmic
CC region, which forms a coiled-coil structure, are required for
CC interaction with FtsL and recruitment of downstream division proteins.
CC The C-terminal region is required for interaction with FtsQ, but is not
CC required for recruitment of the downstream division protein FtsI.
CC Contains a leucine zipper-like (LZ) motif, which is required for
CC optimal interaction with FtsL. {ECO:0000269|PubMed:19233928,
CC ECO:0000269|PubMed:21784946}.
CC -!- DISRUPTION PHENOTYPE: Mutants form long filaments, but DNA segregation
CC is not affected. {ECO:0000269|PubMed:11972052}.
CC -!- MISCELLANEOUS: The C-terminal domain of FtsB is degraded in the absence
CC of either FtsL or FtsQ.
CC -!- SIMILARITY: Belongs to the FtsB family. {ECO:0000255|HAMAP-
CC Rule:MF_00599}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U29579; AAA69258.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75790.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76825.1; -; Genomic_DNA.
DR PIR; H65055; H65055.
DR RefSeq; NP_417228.1; NC_000913.3.
DR RefSeq; WP_000517476.1; NZ_STEB01000027.1.
DR PDB; 4IFF; X-ray; 2.30 A; A/B/C/D=28-63.
DR PDB; 5Z2W; X-ray; 3.00 A; B=61-95.
DR PDBsum; 4IFF; -.
DR PDBsum; 5Z2W; -.
DR AlphaFoldDB; P0A6S5; -.
DR SMR; P0A6S5; -.
DR BioGRID; 4262281; 273.
DR BioGRID; 850394; 2.
DR ComplexPortal; CPX-3099; FtsQBL complex.
DR ComplexPortal; CPX-3299; FtsBL complex.
DR DIP; DIP-12117N; -.
DR IntAct; P0A6S5; 8.
DR STRING; 511145.b2748; -.
DR PaxDb; P0A6S5; -.
DR PRIDE; P0A6S5; -.
DR EnsemblBacteria; AAC75790; AAC75790; b2748.
DR EnsemblBacteria; BAE76825; BAE76825; BAE76825.
DR GeneID; 66673378; -.
DR GeneID; 946033; -.
DR KEGG; ecj:JW2718; -.
DR KEGG; eco:b2748; -.
DR PATRIC; fig|1411691.4.peg.3992; -.
DR EchoBASE; EB2914; -.
DR eggNOG; COG2919; Bacteria.
DR HOGENOM; CLU_134863_5_2_6; -.
DR InParanoid; P0A6S5; -.
DR OMA; YELGMVK; -.
DR PhylomeDB; P0A6S5; -.
DR BioCyc; EcoCyc:G7424-MON; -.
DR PRO; PR:P0A6S5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032153; C:cell division site; IC:ComplexPortal.
DR GO; GO:0030428; C:cell septum; IDA:EcoliWiki.
DR GO; GO:1990586; C:divisome complex; IPI:ComplexPortal.
DR GO; GO:1990588; C:FtsBL complex; IC:ComplexPortal.
DR GO; GO:1990587; C:FtsQBL complex; IPI:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0051301; P:cell division; IMP:EcoliWiki.
DR GO; GO:0000917; P:division septum assembly; IC:ComplexPortal.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IMP:EcoCyc.
DR HAMAP; MF_00599; FtsB; 1.
DR InterPro; IPR023081; Cell_div_FtsB.
DR InterPro; IPR007060; FtsL/DivIC.
DR PANTHER; PTHR37485; PTHR37485; 1.
DR Pfam; PF04977; DivIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cell inner membrane;
KW Cell membrane; Coiled coil; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..103
FT /note="Cell division protein FtsB"
FT /id="PRO_0000214441"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00599"
FT TRANSMEM 4..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00599"
FT TOPO_DOM 22..103
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00599"
FT COILED 31..71
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00599"
FT MOTIF 41..72
FT /note="Leucine zipper-like"
FT HELIX 28..59
FT /evidence="ECO:0007829|PDB:4IFF"
FT HELIX 63..75
FT /evidence="ECO:0007829|PDB:5Z2W"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:5Z2W"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:5Z2W"
SQ SEQUENCE 103 AA; 11622 MW; 9B50A7EF637809D7 CRC64;
MGKLTLLLLA ILVWLQYSLW FGKNGIHDYT RVNDDVAAQQ ATNAKLKARN DQLFAEIDDL
NGGQEALEER ARNELSMTRP GETFYRLVPD ASKRAQSAGQ NNR
