FTSE_SHIFL
ID FTSE_SHIFL Reviewed; 222 AA.
AC P0A9S0; P10115;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Cell division ATP-binding protein FtsE;
GN Name=ftsE; OrderedLocusNames=SF3481, S4282;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN44940.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP19242.1; -; Genomic_DNA.
DR RefSeq; NP_709233.2; NC_004337.2.
DR RefSeq; WP_000617723.1; NZ_WPGW01000010.1.
DR AlphaFoldDB; P0A9S0; -.
DR SMR; P0A9S0; -.
DR STRING; 198214.SF3481; -.
DR PRIDE; P0A9S0; -.
DR EnsemblBacteria; AAN44940; AAN44940; SF3481.
DR EnsemblBacteria; AAP19242; AAP19242; S4282.
DR GeneID; 1026428; -.
DR GeneID; 67417092; -.
DR KEGG; sfl:SF3481; -.
DR KEGG; sfx:S4282; -.
DR PATRIC; fig|198214.7.peg.4102; -.
DR HOGENOM; CLU_000604_1_22_6; -.
DR OMA; PTRGHID; -.
DR OrthoDB; 1181903at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; Reference proteome.
FT CHAIN 1..222
FT /note="Cell division ATP-binding protein FtsE"
FT /id="PRO_0000092332"
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