SAPB_SALTY
ID SAPB_SALTY Reviewed; 321 AA.
AC P0A2J3; P36668;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Peptide transport system permease protein SapB;
GN Name=sapB {ECO:0000303|PubMed:8223423}; OrderedLocusNames=STM1693;
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, AND OPERON STRUCTURE.
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:0000250}; Multi-pass
CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- INDUCTION: Part of the sapA-sapB-sapC-sapD-sapF operon, RNA detected in
CC mid-log phase cells. {ECO:0000269|PubMed:8223423}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. OppBC subfamily. {ECO:0000305}.
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DR EMBL; X74212; CAA52285.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20610.1; -; Genomic_DNA.
DR PIR; S39586; S39586.
DR RefSeq; NP_460651.1; NC_003197.2.
DR RefSeq; WP_000583298.1; NC_003197.2.
DR AlphaFoldDB; P0A2J3; -.
DR STRING; 99287.STM1693; -.
DR TCDB; 3.A.1.5.5; the atp-binding cassette (abc) superfamily.
DR PaxDb; P0A2J3; -.
DR EnsemblBacteria; AAL20610; AAL20610; STM1693.
DR GeneID; 1253211; -.
DR KEGG; stm:STM1693; -.
DR PATRIC; fig|99287.12.peg.1787; -.
DR HOGENOM; CLU_036879_0_3_6; -.
DR OMA; RKEWYAN; -.
DR PhylomeDB; P0A2J3; -.
DR BioCyc; SENT99287:STM1693-MON; -.
DR Proteomes; UP000001014; 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:0071916; F:dipeptide transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Membrane; Peptide transport;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..321
FT /note="Peptide transport system permease protein SapB"
FT /id="PRO_0000060161"
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"
FT CONFLICT 97..98
FT /note="ML -> TV (in Ref. 1; CAA52285)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="S -> C (in Ref. 1; CAA52285)"
FT /evidence="ECO:0000305"
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
