ID   SAPF_ECOL6              Reviewed;         268 AA.
AC   P0AAH9; P36637;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Peptide transport system ATP-binding protein SapF;
GN   Name=sapF; OrderedLocusNames=c1767;
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: Involved in a peptide intake transport system that plays a
CC       role in the resistance to antimicrobial peptides. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; AE014075; AAN80233.1; -; Genomic_DNA.
DR   RefSeq; WP_000573407.1; NC_004431.1.
DR   AlphaFoldDB; P0AAH9; -.
DR   SMR; P0AAH9; -.
DR   STRING; 199310.c1767; -.
DR   EnsemblBacteria; AAN80233; AAN80233; c1767.
DR   GeneID; 66674883; -.
DR   KEGG; ecc:c1767; -.
DR   eggNOG; COG4172; Bacteria.
DR   HOGENOM; CLU_000604_1_23_6; -.
DR   OMA; PEIDRKW; -.
DR   BioCyc; ECOL199310:C1767-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:0015833; P:peptide transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; 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; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Peptide transport; Protein transport; Transport.
FT   CHAIN           1..268
FT                   /note="Peptide transport system ATP-binding protein SapF"
FT                   /id="PRO_0000092969"
FT   DOMAIN          6..251
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         47..54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   268 AA;  30571 MW;  F3B98BC9DC6DCBFA CRC64;
     MIETLLEVRN LSKTFRYRTG WFRRQTVEAV KPLSFTLREG QTLAIIGENG SGKSTLAKML
     AGMIEPTSGE LLIDDHPLHF GDYSFRSQRI RMIFQDPSTS LNPRQRISQI LDFPLRLNTD
     LEPEQRRKQI IETMRMVGLL PDHVSYYPHM LAPGQKQRLG LARALILRPK VIIADEALAS
     LDMSMRSQLI NLMLELQEKQ GISYIYVTQH IGMMKHISDQ VLVMHQGEVV ERGSTADVLA
     SPLHELTKRL IAGHFGEALT ADAWRKDR