ID   SAPD_SALTY              Reviewed;         330 AA.
AC   P36636;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Peptide transport system ATP-binding protein SapD;
GN   Name=sapD {ECO:0000303|PubMed:8223423}; OrderedLocusNames=STM1695;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, OPERON STRUCTURE, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 14028s / SGSG 2262;
RX   PubMed=8223423; DOI=10.1002/j.1460-2075.1993.tb06089.x;
RA   Parra-Lopez C., Baer M.T., Groisman E.A.;
RT   "Molecular genetic analysis of a locus required for resistance to
RT   antimicrobial peptides in Salmonella typhimurium.";
RL   EMBO J. 12:4053-4062(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Involved in a peptide intake transport system that plays a
CC       role in the resistance to antimicrobial peptides.
CC       {ECO:0000269|PubMed:8223423}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC       membrane protein {ECO:0000305}.
CC   -!- INDUCTION: Part of the sapA-sapB-sapC-sapD-sapF operon, RNA detected in
CC       mid-log phase cells. {ECO:0000269|PubMed:8223423}.
CC   -!- DISRUPTION PHENOTYPE: Loss of resistance to protamine.
CC       {ECO:0000269|PubMed:8223423}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X74212; CAA52287.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20612.1; -; Genomic_DNA.
DR   PIR; S39588; S39588.
DR   RefSeq; NP_460653.1; NC_003197.2.
DR   RefSeq; WP_001128868.1; NC_003197.2.
DR   AlphaFoldDB; P36636; -.
DR   SMR; P36636; -.
DR   STRING; 99287.STM1695; -.
DR   TCDB; 3.A.1.5.5; the atp-binding cassette (abc) superfamily.
DR   PaxDb; P36636; -.
DR   EnsemblBacteria; AAL20612; AAL20612; STM1695.
DR   GeneID; 1253213; -.
DR   KEGG; stm:STM1695; -.
DR   PATRIC; fig|99287.12.peg.1789; -.
DR   HOGENOM; CLU_000604_1_23_6; -.
DR   OMA; PHGRVKA; -.
DR   PhylomeDB; P36636; -.
DR   BioCyc; SENT99287:STM1695-MON; -.
DR   Proteomes; UP000001014; 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   2: Evidence at transcript level;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Peptide transport; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..330
FT                   /note="Peptide transport system ATP-binding protein SapD"
FT                   /id="PRO_0000092965"
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"
FT   CONFLICT        150..151
FT                   /note="DA -> EP (in Ref. 1; CAA52287)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   330 AA;  37572 MW;  11E7267B431ED0E9 CRC64;
     MPLLDIRNLT IEFKTSEGWV KAVDRVSMTL SEGEIRGLVG ESGSGKSLIA KAICGVAKDN
     WRVTADRMRF DDIDLLRLSS RERRKLVGHN VSMIFQEPQS CLDPSERVGR QLMQNIPAWT
     YKGRWWQRLG WRKRRAIELL HRVGIKDHKD AMRSFPYELT DGECQKVMIA IALANQPRLL
     IADEPTNSME PTTQAQIFRL LTRLNQNSNT TILLISHDLQ MLSQWADKIN VLYCGQTVET
     APSKDLVTMP HHPYTQALIR AIPDFGSAMP HKSRLNTLPG AIPLLEQLPI GCRLGPRCPY
     AQRECIITPR LTGAKNHLYA CHFPLNMERE