ID   SAPB_SALTI              Reviewed;         321 AA.
AC   P0A2J4; P36668;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Peptide transport system permease protein SapB;
GN   Name=sapB; OrderedLocusNames=STY1368, t1598;
OS   Salmonella typhi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT18;
RX   PubMed=11677608; DOI=10.1038/35101607;
RA   Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA   Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA   Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA   Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA   Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA   Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA   Barrell B.G.;
RT   "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT   serovar Typhi CT18.";
RL   Nature 413:848-852(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700931 / Ty2;
RX   PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA   Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA   Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT   "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT   CT18.";
RL   J. Bacteriol. 185:2330-2337(2003).
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:0000250}; Multi-pass
CC       membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. OppBC subfamily. {ECO:0000305}.
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DR   EMBL; AL513382; CAD01636.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO69229.1; -; Genomic_DNA.
DR   RefSeq; NP_455810.1; NC_003198.1.
DR   RefSeq; WP_000583298.1; NZ_WSUR01000006.1.
DR   AlphaFoldDB; P0A2J4; -.
DR   STRING; 220341.16502488; -.
DR   EnsemblBacteria; AAO69229; AAO69229; t1598.
DR   KEGG; stt:t1598; -.
DR   KEGG; sty:STY1368; -.
DR   PATRIC; fig|220341.7.peg.1377; -.
DR   eggNOG; COG4168; Bacteria.
DR   HOGENOM; CLU_036879_0_3_6; -.
DR   OMA; RKEWYAN; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd06261; TM_PBP2; 1.
DR   Gene3D; 1.10.3720.10; -; 1.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   SUPFAM; SSF161098; SSF161098; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Peptide transport;
KW   Protein transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..321
FT                   /note="Peptide transport system permease protein SapB"
FT                   /id="PRO_0000060160"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        30..80
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        102..113
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        135..174
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        196..248
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        249..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        270..280
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TOPO_DOM        302..321
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          74..302
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   321 AA;  36111 MW;  8A84AF71282E95F9 CRC64;
     MIIFTLRRLL LLLVTLFFLT FIGFSLSYFT PHAPLQGASL WNAWVFWFNG LLHWDFGVSS
     INGQLISEQL KEVFPATMEL CILAFGFALM VGIPVGMLAG VTRSKWPDRF ISALALLGFS
     IPVFWLALLL TLFFSLTLGW LPVSGRFDLL YEVKPVTGFA IIDAWISDSP WRDEMVMSAI
     RHMVLPVLTL SVAPTTEVIR LMRISTIEVY DQNYVKAAAT RGLSRFTILR RHVLHNALPP
     VIPRLGLQFS TMLTLAMITE MVFSWPGLGR WLIHAIRQQD YAAISAGVMV IGSLVIVVNV
     ISDILGAMAN PLKHKEWYAL R