ID   SAPA_SALTY              Reviewed;         549 AA.
AC   P36634;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Peptide transport periplasmic protein SapA;
DE   Flags: Precursor;
GN   Name=sapA {ECO:0000303|PubMed:8223423}; OrderedLocusNames=STM1692;
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: Periplasm {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: More senstitive to protamine than wild-type
CC       cells, but not as sensitive as sapC, sapD or sapF deletions.
CC       {ECO:0000269|PubMed:8223423}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC       {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; CAA52284.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20609.1; -; Genomic_DNA.
DR   PIR; S39585; S39585.
DR   RefSeq; NP_460650.1; NC_003197.2.
DR   RefSeq; WP_001241629.1; NC_003197.2.
DR   AlphaFoldDB; P36634; -.
DR   SMR; P36634; -.
DR   STRING; 99287.STM1692; -.
DR   TCDB; 3.A.1.5.5; the atp-binding cassette (abc) superfamily.
DR   PaxDb; P36634; -.
DR   EnsemblBacteria; AAL20609; AAL20609; STM1692.
DR   GeneID; 1253210; -.
DR   KEGG; stm:STM1692; -.
DR   PATRIC; fig|99287.12.peg.1786; -.
DR   HOGENOM; CLU_017028_7_0_6; -.
DR   OMA; NQYVRLV; -.
DR   PhylomeDB; P36634; -.
DR   BioCyc; SENT99287:STM1692-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR   GO; GO:1904680; F:peptide transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015833; P:peptide transport; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR030678; Peptide/Ni-bd.
DR   InterPro; IPR039424; SBP_5.
DR   InterPro; IPR023765; SBP_5_CS.
DR   InterPro; IPR000914; SBP_5_dom.
DR   PANTHER; PTHR30290; PTHR30290; 1.
DR   Pfam; PF00496; SBP_bac_5; 1.
DR   PIRSF; PIRSF002741; MppA; 1.
DR   PROSITE; PS01040; SBP_BACTERIAL_5; 1.
PE   2: Evidence at transcript level;
KW   Peptide transport; Periplasm; Protein transport; Reference proteome;
KW   Signal; Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..549
FT                   /note="Peptide transport periplasmic protein SapA"
FT                   /id="PRO_0000031802"
FT   CONFLICT        164..165
FT                   /note="KL -> NV (in Ref. 1; CAA52284)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   549 AA;  61651 MW;  B1C2981DE661CEDE CRC64;
     MRLVLSSLIV IAGLLSSQAT AATAPEQTAS ADIRDSGFVY CVSGQVNTFN PQKASSGLIV
     DTLAAQLYDR LLDVDPYTYR LVPELAESWE VLDNGATYRF HLRRDVSFQK TAWFTPTRKL
     NADDVVFTFQ RIFDRRHPWH NINGSSFPYF DSLQFADNVK SVRKLDNNTV EFRLTQPDAS
     FLWHLATHYA SVMSAEYAAQ LSRKDRQELL DRQPVGTGPF QLSEYRAGQF IRLQRHDGFW
     RGKPLMPQVV VDLGSGGTGR LSKLLTGECD VLAWPAASQL TILRDDPRLR LTLRPGMNIA
     YLAFNTDKPP LNNPAVRHAL ALSINNQRLM QSIYYGTAET AASILPRASW AYDNDAKITE
     YNPQKSREQL KALGIENLTL HLWVPTSSQA WNPSPLKTAE LIQADMAQVG VKVVIVPVEG
     RFQEARLMDM NHDLTLSGWA TDSNDPDSFF RPLLSCAAIN SQTNFAHWCN PEFDSVLRKA
     LSSQQLASRI EAYEEAQNIL EKELPILPLA SSLRLQAYRY DIKGLVLSPF GNASFAGVSR
     EKHEEVKKP