FTSA_ECOLI
ID FTSA_ECOLI Reviewed; 420 AA.
AC P0ABH0; P06137; Q47229;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Cell division protein FtsA {ECO:0000255|HAMAP-Rule:MF_02033};
GN Name=ftsA {ECO:0000255|HAMAP-Rule:MF_02033}; Synonyms=divA;
GN OrderedLocusNames=b0094, JW0092;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6094474; DOI=10.1128/jb.160.2.546-555.1984;
RA Robinson A.C., Kenan D.J., Hatfull G.F., Sullivan N.F., Spiegelberg R.,
RA Donachie W.D.;
RT "DNA sequence and transcriptional organization of essential cell division
RT genes ftsQ and ftsA of Escherichia coli: evidence for overlapping
RT transcriptional units.";
RL J. Bacteriol. 160:546-555(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2995680; DOI=10.1016/0022-2836(85)90290-6;
RA Yi Q.-M., Rockenbach S., Ward J.E. Jr., Lutkenhaus J.;
RT "Structure and expression of the cell division genes ftsQ, ftsA and ftsZ.";
RL J. Mol. Biol. 184:399-412(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANTS TEMPERATURE-SENSITIVE.
RX PubMed=2846985; DOI=10.1111/j.1365-2958.1988.tb00066.x;
RA Robinson A.C., Begg K.J., Sweeney J., Condie A., Donachie W.D.;
RT "Mapping and characterization of mutants of the Escherichia coli cell
RT division gene, ftsA.";
RL Mol. Microbiol. 2:581-588(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-116.
RX PubMed=2228979; DOI=10.1128/jb.172.11.6611-6614.1990;
RA Dewar S.J., Donachie W.D.;
RT "Regulation of expression of the ftsA cell division gene by sequences in
RT upstream genes.";
RL J. Bacteriol. 172:6611-6614(1990).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 318-420.
RC STRAIN=K12;
RX PubMed=3000876; DOI=10.1016/0378-1119(85)90179-9;
RA Yi Q.-M., Lutkenhaus J.;
RT "The nucleotide sequence of the essential cell-division gene ftsZ of
RT Escherichia coli.";
RL Gene 36:241-247(1985).
RN [9]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / ATCC 35607 / JM83;
RX PubMed=2203741; DOI=10.1128/jb.172.9.5097-5102.1990;
RA Pla J., Dopazo A., Vicente M.;
RT "The native form of FtsA, a septal protein of Escherichia coli, is located
RT in the cytoplasmic membrane.";
RL J. Bacteriol. 172:5097-5102(1990).
RN [10]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=8955398; DOI=10.1128/jb.178.24.7167-7172.1996;
RA Addinall S.G., Lutkenhaus J.;
RT "FtsA is localized to the septum in an FtsZ-dependent manner.";
RL J. Bacteriol. 178:7167-7172(1996).
RN [11]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH FTSZ.
RX PubMed=8917533; DOI=10.1073/pnas.93.23.12998;
RA Ma X., Ehrhardt D.W., Margolin W.;
RT "Colocalization of cell division proteins FtsZ and FtsA to cytoskeletal
RT structures in living Escherichia coli cells by using green fluorescent
RT protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:12998-13003(1996).
RN [12]
RP FUNCTION IN RECRUITMENT OF FTSN.
RC STRAIN=K12;
RX PubMed=9282742; DOI=10.1046/j.1365-2958.1997.4641833.x;
RA Addinall S.G., Cao C., Lutkenhaus J.;
RT "FtsN, a late recruit to the septum in Escherichia coli.";
RL Mol. Microbiol. 25:303-309(1997).
RN [13]
RP FUNCTION IN RECRUITMENT OF FTSK, AND SUBCELLULAR LOCATION.
RX PubMed=9495771; DOI=10.1128/jb.180.5.1296-1304.1998;
RA Yu X.C., Tran A.H., Sun Q., Margolin W.;
RT "Localization of cell division protein FtsK to the Escherichia coli septum
RT and identification of a potential N-terminal targeting domain.";
RL J. Bacteriol. 180:1296-1304(1998).
RN [14]
RP FUNCTION IN RECRUITMENT OF FTSI.
RX PubMed=9603865; DOI=10.1128/jb.180.11.2810-2816.1998;
RA Wang L., Khattar M.K., Donachie W.D., Lutkenhaus J.;
RT "FtsI and FtsW are localized to the septum in Escherichia coli.";
RL J. Bacteriol. 180:2810-2816(1998).
RN [15]
RP FUNCTION IN RECRUITMENT OF FTSQ.
RX PubMed=9882666; DOI=10.1128/jb.181.2.521-530.1999;
RA Chen J.C., Weiss D.S., Ghigo J.M., Beckwith J.;
RT "Septal localization of FtsQ, an essential cell division protein in
RT Escherichia coli.";
RL J. Bacteriol. 181:521-530(1999).
RN [16]
RP FUNCTION IN RECRUITMENT OF FTSL.
RX PubMed=10027987; DOI=10.1046/j.1365-2958.1999.01213.x;
RA Ghigo J.M., Weiss D.S., Chen J.C., Yarrow J.C., Beckwith J.;
RT "Localization of FtsL to the Escherichia coli septal ring.";
RL Mol. Microbiol. 31:725-737(1999).
RN [17]
RP FUNCTION, ATP-BINDING, SUBUNIT, DOMAIN, AND MUTAGENESIS OF ASP-210.
RX PubMed=11053380; DOI=10.1128/jb.182.22.6366-6373.2000;
RA Yim L., Vandenbussche G., Mingorance J., Rueda S., Casanova M.,
RA Ruysschaert J.M., Vicente M.;
RT "Role of the carboxy terminus of Escherichia coli FtsA in self-interaction
RT and cell division.";
RL J. Bacteriol. 182:6366-6373(2000).
RN [18]
RP FUNCTION.
RX PubMed=11847116; DOI=10.1093/emboj/21.4.685;
RA Pichoff S., Lutkenhaus J.;
RT "Unique and overlapping roles for ZipA and FtsA in septal ring assembly in
RT Escherichia coli.";
RL EMBO J. 21:685-693(2002).
RN [19]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF TRP-408;
RP ILE-409; ARG-411; LEU-412; TRP-415; LEU-416 AND PHE-420.
RC STRAIN=K12;
RX PubMed=15752196; DOI=10.1111/j.1365-2958.2005.04522.x;
RA Pichoff S., Lutkenhaus J.;
RT "Tethering the Z ring to the membrane through a conserved membrane
RT targeting sequence in FtsA.";
RL Mol. Microbiol. 55:1722-1734(2005).
RN [20]
RP INTERACTION WITH FTSZ AND SELF-INTERACTION.
RX PubMed=17501933; DOI=10.1111/j.1365-2958.2007.05735.x;
RA Pichoff S., Lutkenhaus J.;
RT "Identification of a region of FtsA required for interaction with FtsZ.";
RL Mol. Microbiol. 64:1129-1138(2007).
RN [21]
RP INTERACTION WITH FTSN.
RX PubMed=22328664; DOI=10.1128/jb.06683-11;
RA Busiek K.K., Eraso J.M., Wang Y., Margolin W.;
RT "The early divisome protein FtsA interacts directly through its 1c
RT subdomain with the cytoplasmic domain of the late divisome protein FtsN.";
RL J. Bacteriol. 194:1989-2000(2012).
RN [22]
RP FUNCTION IN RECRUITMENT OF FTSN, AND INTERACTION WITH FTSN.
RX PubMed=24750258; DOI=10.1111/mmi.12623;
RA Busiek K.K., Margolin W.;
RT "A role for FtsA in SPOR-independent localization of the essential
RT Escherichia coli cell division protein FtsN.";
RL Mol. Microbiol. 92:1212-1226(2014).
CC -!- FUNCTION: Essential cell division protein that assists in the assembly
CC of the Z ring (PubMed:11847116). May serve as the principal membrane
CC anchor for the Z ring (PubMed:15752196). Also required for the
CC recruitment to the septal ring of the downstream cell division proteins
CC FtsK, FtsQ, FtsL, FtsI and FtsN (PubMed:9282742, PubMed:9495771,
CC PubMed:9603865, PubMed:9882666, PubMed:10027987, PubMed:24750258).
CC Binds ATP (PubMed:11053380). {ECO:0000269|PubMed:10027987,
CC ECO:0000269|PubMed:11053380, ECO:0000269|PubMed:11847116,
CC ECO:0000269|PubMed:15752196, ECO:0000269|PubMed:24750258,
CC ECO:0000269|PubMed:9282742, ECO:0000269|PubMed:9495771,
CC ECO:0000269|PubMed:9603865, ECO:0000269|PubMed:9882666}.
CC -!- SUBUNIT: Self-interacts (PubMed:11053380, PubMed:17501933). Interacts
CC with FtsZ. This interaction plays an essential role in cell division
CC (PubMed:8917533, PubMed:17501933). Interacts directly with the
CC cytoplasmic region of FtsN (PubMed:22328664, PubMed:24750258).
CC {ECO:0000269|PubMed:11053380, ECO:0000269|PubMed:17501933,
CC ECO:0000269|PubMed:22328664, ECO:0000269|PubMed:24750258,
CC ECO:0000269|PubMed:8917533}.
CC -!- INTERACTION:
CC P0ABH0; P0ABH0: ftsA; NbExp=4; IntAct=EBI-550562, EBI-550562;
CC P0ABH0; P29131: ftsN; NbExp=7; IntAct=EBI-550562, EBI-1134233;
CC P0ABH0; P0A9A6: ftsZ; NbExp=8; IntAct=EBI-550562, EBI-370963;
CC P0ABH0; P0A9X4: mreB; NbExp=3; IntAct=EBI-550562, EBI-371008;
CC P0ABH0; P0ADX7: yhhA; NbExp=3; IntAct=EBI-550562, EBI-550623;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15752196,
CC ECO:0000269|PubMed:2203741}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15752196, ECO:0000269|PubMed:2203741}; Cytoplasmic
CC side {ECO:0000269|PubMed:15752196, ECO:0000269|PubMed:2203741}.
CC Note=Localizes to the Z ring in an FtsZ-dependent manner
CC (PubMed:8955398, PubMed:8917533, PubMed:9495771). Targeted to the
CC membrane through a conserved C-terminal amphipathic helix
CC (PubMed:15752196). {ECO:0000269|PubMed:15752196,
CC ECO:0000269|PubMed:8917533, ECO:0000269|PubMed:8955398,
CC ECO:0000269|PubMed:9495771}.
CC -!- DOMAIN: The extreme C-terminus is essential for localization to the
CC membrane and the Z ring, self-interaction and activity.
CC {ECO:0000269|PubMed:11053380, ECO:0000269|PubMed:15752196}.
CC -!- SIMILARITY: Belongs to the FtsA/MreB family. {ECO:0000255|HAMAP-
CC Rule:MF_02033, ECO:0000305}.
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; K02668; AAA23817.1; -; Genomic_DNA.
DR EMBL; M36531; AAA23811.1; -; Genomic_DNA.
DR EMBL; X55034; CAA38871.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73205.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96662.1; -; Genomic_DNA.
DR PIR; B23318; CEECA.
DR RefSeq; NP_414636.1; NC_000913.3.
DR RefSeq; WP_000588474.1; NZ_STEB01000010.1.
DR AlphaFoldDB; P0ABH0; -.
DR SMR; P0ABH0; -.
DR BioGRID; 4261886; 382.
DR BioGRID; 849180; 1.
DR ComplexPortal; CPX-1936; Divisome complex.
DR DIP; DIP-47983N; -.
DR IntAct; P0ABH0; 27.
DR MINT; P0ABH0; -.
DR STRING; 511145.b0094; -.
DR ChEMBL; CHEMBL3309010; -.
DR jPOST; P0ABH0; -.
DR PaxDb; P0ABH0; -.
DR PRIDE; P0ABH0; -.
DR EnsemblBacteria; AAC73205; AAC73205; b0094.
DR EnsemblBacteria; BAB96662; BAB96662; BAB96662.
DR GeneID; 67416167; -.
DR GeneID; 944778; -.
DR KEGG; ecj:JW0092; -.
DR KEGG; eco:b0094; -.
DR PATRIC; fig|1411691.4.peg.2186; -.
DR EchoBASE; EB0335; -.
DR eggNOG; COG0849; Bacteria.
DR HOGENOM; CLU_037850_3_2_6; -.
DR InParanoid; P0ABH0; -.
DR OMA; DGIIRHT; -.
DR PhylomeDB; P0ABH0; -.
DR BioCyc; EcoCyc:EG10339-MON; -.
DR PRO; PR:P0ABH0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032153; C:cell division site; IDA:EcoliWiki.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1990586; C:divisome complex; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IMP: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; IC:ComplexPortal.
DR HAMAP; MF_02033; FtsA; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR020823; Cell_div_FtsA.
DR InterPro; IPR003494; SHS2_FtsA.
DR Pfam; PF02491; SHS2_FTSA; 1.
DR PIRSF; PIRSF003101; FtsA; 1.
DR SMART; SM00842; FtsA; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR01174; ftsA; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome.
FT CHAIN 1..420
FT /note="Cell division protein FtsA"
FT /id="PRO_0000062734"
FT MUTAGEN 210
FT /note="D->A: Does not bind ATP."
FT /evidence="ECO:0000269|PubMed:11053380"
FT MUTAGEN 408
FT /note="W->E: Prevents localization to the Z ring. Lack of
FT activity."
FT /evidence="ECO:0000269|PubMed:15752196"
FT MUTAGEN 409
FT /note="I->E: Prevents localization to the Z ring. Lack of
FT activity."
FT /evidence="ECO:0000269|PubMed:15752196"
FT MUTAGEN 411
FT /note="R->E: Does not affect localization or function."
FT /evidence="ECO:0000269|PubMed:15752196"
FT MUTAGEN 412
FT /note="L->E: Prevents localization to the Z ring. Lack of
FT activity."
FT /evidence="ECO:0000269|PubMed:15752196"
FT MUTAGEN 415
FT /note="W->E: Prevents localization to the Z ring. Lack of
FT activity."
FT /evidence="ECO:0000269|PubMed:15752196"
FT MUTAGEN 416
FT /note="L->E: Prevents localization to the Z ring. Lack of
FT activity."
FT /evidence="ECO:0000269|PubMed:15752196"
FT MUTAGEN 420
FT /note="F->E: Does not affect localization or function."
FT /evidence="ECO:0000269|PubMed:15752196"
FT CONFLICT 339
FT /note="A -> R (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 45330 MW; C2475377A229B982 CRC64;
MIKATDRKLV VGLEIGTAKV AALVGEVLPD GMVNIIGVGS CPSRGMDKGG VNDLESVVKC
VQRAIDQAEL MADCQISSVY LALSGKHISC QNEIGMVPIS EEEVTQEDVE NVVHTAKSVR
VRDEHRVLHV IPQEYAIDYQ EGIKNPVGLS GVRMQAKVHL ITCHNDMAKN IVKAVERCGL
KVDQLIFAGL ASSYSVLTED ERELGVCVVD IGGGTMDIAV YTGGALRHTK VIPYAGNVVT
SDIAYAFGTP PSDAEAIKVR HGCALGSIVG KDESVEVPSV GGRPPRSLQR QTLAEVIEPR
YTELLNLVNE EILQLQEKLR QQGVKHHLAA GIVLTGGAAQ IEGLAACAQR VFHTQVRIGA
PLNITGLTDY AQEPYYSTAV GLLHYGKESH LNGEAEVEKR VTASVGSWIK RLNSWLRKEF
