FTSE_ECOLI
ID FTSE_ECOLI Reviewed; 222 AA.
AC P0A9R7; P10115; Q2M7C6;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Cell division ATP-binding protein FtsE {ECO:0000305};
GN Name=ftsE; OrderedLocusNames=b3463, JW3428;
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=3025556; DOI=10.1007/bf02428043;
RA Gill D.R., Hatfull G.F., Salmond G.P.C.;
RT "A new cell division operon in Escherichia coli.";
RL Mol. Gen. Genet. 205:134-145(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
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 [4]
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=3323846; DOI=10.1007/bf00327204;
RA Gill D.R., Salmond G.P.;
RT "The Escherichia coli cell division proteins FtsY, FtsE and FtsX are inner
RT membrane-associated.";
RL Mol. Gen. Genet. 210:504-508(1987).
RN [6]
RP SUBUNIT, INTERACTION WITH FTSX, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP ATP-BINDING, AND MUTAGENESIS OF LYS-41 AND CYS-49.
RX PubMed=10048040; DOI=10.1046/j.1365-2958.1999.01245.x;
RA de Leeuw E., Graham B., Phillips G.J., ten Hagen-Jongman C.M., Oudega B.,
RA Luirink J.;
RT "Molecular characterization of Escherichia coli FtsE and FtsX.";
RL Mol. Microbiol. 31:983-993(1999).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=14729705; DOI=10.1128/jb.186.3.785-793.2004;
RA Schmidt K.L., Peterson N.D., Kustusch R.J., Wissel M.C., Graham B.,
RA Phillips G.J., Weiss D.S.;
RT "A predicted ABC transporter, FtsEX, is needed for cell division in
RT Escherichia coli.";
RL J. Bacteriol. 186:785-793(2004).
RN [8]
RP INTERACTION WITH FTSZ.
RX PubMed=17307852; DOI=10.1128/jb.01581-06;
RA Corbin B.D., Wang Y., Beuria T.K., Margolin W.;
RT "Interaction between cell division proteins FtsE and FtsZ.";
RL J. Bacteriol. 189:3026-3035(2007).
CC -!- FUNCTION: Part of the ABC transporter FtsEX involved in cellular
CC division. Important for assembly or stability of the septal ring.
CC {ECO:0000269|PubMed:14729705}.
CC -!- SUBUNIT: Homodimer (PubMed:10048040). Forms a membrane-associated
CC complex with FtsX (PubMed:10048040). Interacts with FtsZ, independently
CC of FtsX, FtsA or ZipA (PubMed:17307852). {ECO:0000269|PubMed:10048040,
CC ECO:0000269|PubMed:17307852}.
CC -!- INTERACTION:
CC P0A9R7; P0A9A6: ftsZ; NbExp=2; IntAct=EBI-550637, EBI-370963;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:10048040,
CC ECO:0000269|PubMed:3323846}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10048040}; Cytoplasmic side {ECO:0000305}.
CC Note=Associated with the membrane through an interaction with FtsX
CC (PubMed:10048040). Localizes to the septal ring at the later stages of
CC cell growth and remains there until division is complete
CC (PubMed:14729705). This localization is dependent on localization of
CC FtsZ, FtsA and ZipA, but not on the downstream division proteins FtsK,
CC FtsQ or FtsI (PubMed:14729705). {ECO:0000269|PubMed:10048040,
CC ECO:0000269|PubMed:14729705}.
CC -!- DISRUPTION PHENOTYPE: Inactivation results in a filamented cellular
CC morphology, but not in a temperature-sensitive phenotype.
CC {ECO:0000269|PubMed:10048040}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; X04398; CAA27985.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18438.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76488.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77830.1; -; Genomic_DNA.
DR PIR; S03131; CEECFE.
DR RefSeq; NP_417920.1; NC_000913.3.
DR RefSeq; WP_000617723.1; NZ_STEB01000004.1.
DR AlphaFoldDB; P0A9R7; -.
DR SMR; P0A9R7; -.
DR BioGRID; 4260774; 393.
DR ComplexPortal; CPX-4602; FtsEX ABC cell division complex.
DR DIP; DIP-47843N; -.
DR IntAct; P0A9R7; 29.
DR STRING; 511145.b3463; -.
DR TCDB; 3.A.1.140.1; the atp-binding cassette (abc) superfamily.
DR jPOST; P0A9R7; -.
DR PaxDb; P0A9R7; -.
DR PRIDE; P0A9R7; -.
DR EnsemblBacteria; AAC76488; AAC76488; b3463.
DR EnsemblBacteria; BAE77830; BAE77830; BAE77830.
DR GeneID; 67417092; -.
DR GeneID; 947968; -.
DR KEGG; ecj:JW3428; -.
DR KEGG; eco:b3463; -.
DR PATRIC; fig|1411691.4.peg.3262; -.
DR EchoBASE; EB0336; -.
DR eggNOG; COG2884; Bacteria.
DR HOGENOM; CLU_000604_1_22_6; -.
DR InParanoid; P0A9R7; -.
DR OMA; CHNLETA; -.
DR PhylomeDB; P0A9R7; -.
DR BioCyc; EcoCyc:FTSE-MON; -.
DR PRO; PR:P0A9R7; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1904949; C:ATPase complex; IPI:ComplexPortal.
DR GO; GO:0032153; C:cell division site; IDA:EcoliWiki.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0000935; C:division septum; IDA:ComplexPortal.
DR GO; GO:1990586; C:divisome complex; IC:ComplexPortal.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:EcoCyc.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:EcoliWiki.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098797; C:plasma membrane protein complex; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IDA:EcoliWiki.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
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 GO; GO:0009254; P:peptidoglycan turnover; IC:ComplexPortal.
DR GO; GO:0051781; P:positive regulation of cell division; IDA:ComplexPortal.
DR GO; GO:0046677; P:response to antibiotic; IMP:EcoliWiki.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR005286; Cell_div_FtsE_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02673; FtsE; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Cell inner membrane; Cell membrane;
KW Membrane; Nucleotide-binding; Reference proteome.
FT CHAIN 1..222
FT /note="Cell division ATP-binding protein FtsE"
FT /id="PRO_0000092328"
FT DOMAIN 2..222
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 35..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:10048040"
FT MUTAGEN 41
FT /note="K->R: Does not bind ATP."
FT /evidence="ECO:0000269|PubMed:10048040"
FT MUTAGEN 49
FT /note="C->A: Prevents dimer formation. Does not alter ATP-
FT binding."
FT /evidence="ECO:0000269|PubMed:10048040"
SQ SEQUENCE 222 AA; 24439 MW; 13CFCDECD8FE7590 CRC64;
MIRFEHVSKA YLGGRQALQG VTFHMQPGEM AFLTGHSGAG KSTLLKLICG IERPSAGKIW
FSGHDITRLK NREVPFLRRQ IGMIFQDHHL LMDRTVYDNV AIPLIIAGAS GDDIRRRVSA
ALDKVGLLDK AKNFPIQLSG GEQQRVGIAR AVVNKPAVLL ADEPTGNLDD ALSEGILRLF
EEFNRVGVTV LMATHDINLI SRRSYRMLTL SDGHLHGGVG HE
