ID   FTSE_ECOL6              Reviewed;         222 AA.
AC   P0A9R8; P10115;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Cell division ATP-binding protein FtsE;
GN   Name=ftsE; OrderedLocusNames=c4256;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Part of the ABC transporter FtsEX involved in cellular
CC       division. Important for assembly or stability of the septal ring.
CC       {ECO:0000250|UniProtKB:P0A9R7}.
CC   -!- SUBUNIT: Homodimer. Forms a membrane-associated complex with FtsX.
CC       {ECO:0000250|UniProtKB:P0A9R7}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P0A9R7}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P0A9R7}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P0A9R7}. Note=Associated with the membrane
CC       through an interaction with FtsX. {ECO:0000250|UniProtKB:P0A9R7}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; AE014075; AAN82692.1; -; Genomic_DNA.
DR   RefSeq; WP_000617723.1; NC_004431.1.
DR   AlphaFoldDB; P0A9R8; -.
DR   SMR; P0A9R8; -.
DR   STRING; 199310.c4256; -.
DR   EnsemblBacteria; AAN82692; AAN82692; c4256.
DR   GeneID; 67417092; -.
DR   KEGG; ecc:c4256; -.
DR   eggNOG; COG2884; Bacteria.
DR   HOGENOM; CLU_000604_1_22_6; -.
DR   OMA; PTRGHID; -.
DR   BioCyc; ECOL199310:C4256-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Cell inner membrane; Cell membrane;
KW   Membrane; Nucleotide-binding.
FT   CHAIN           1..222
FT                   /note="Cell division ATP-binding protein FtsE"
FT                   /id="PRO_0000092330"
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:0000255|PROSITE-ProRule:PRU00434"
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