ID   SAPD_ECOL6              Reviewed;         330 AA.
AC   P0AAH5; P36635;
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 SapD;
GN   Name=sapD; OrderedLocusNames=c1768;
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; AAN80234.1; -; Genomic_DNA.
DR   RefSeq; WP_001128858.1; NC_004431.1.
DR   AlphaFoldDB; P0AAH5; -.
DR   SMR; P0AAH5; -.
DR   STRING; 199310.c1768; -.
DR   EnsemblBacteria; AAN80234; AAN80234; c1768.
DR   GeneID; 67417384; -.
DR   KEGG; ecc:c1768; -.
DR   eggNOG; COG4172; Bacteria.
DR   HOGENOM; CLU_000604_1_23_6; -.
DR   OMA; PHGRVKA; -.
DR   BioCyc; ECOL199310:C1768-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; IPR013563; Oligopep_ABC_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF08352; oligo_HPY; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01727; oligo_HPY; 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..330
FT                   /note="Peptide transport system ATP-binding protein SapD"
FT                   /id="PRO_0000092964"
FT   DOMAIN          6..259
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   330 AA;  37661 MW;  1326280E475628E0 CRC64;
     MPLLDIRNLT IEFKTGDEWV KAVDRVSMTL TEGEIRGLVG ESGSGKSLIA KAICGVNKDN
     WRVTADRMRF DDIDLLRLSA RERRKLVGHN VSMIFQEPQS CLDPSERVGR QLMQNIPAWT
     YKGRWWQRFG WRKRRAIELL HRVGIKDHKD AMRSFPYELT EGECQKVMIA IALANQPRLL
     IADEPTNSME PTTQAQIFRL LTRLNQNSNT TILLISHDLQ MLSQWADKIN VLYCGQTVET
     APSKELVTMP HHPYTQALIR AIPDFGSAMP HKSRLNTLPG AIPLLEQLPI GCRLGPRCPY
     AQRECIVTPR LTGAKNHLYA CHFPLNMEKE