ID   THIB_SALTY              Reviewed;         327 AA.
AC   Q7CR85;
DT   11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Thiamine-binding periplasmic protein {ECO:0000305};
DE   Flags: Precursor;
GN   Name=thiB {ECO:0000303|PubMed:9535878};
GN   Synonyms=tbpA {ECO:0000312|EMBL:AAL19072.1};
GN   OrderedLocusNames=STM0108 {ECO:0000312|EMBL:AAL19072.1};
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 [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).
RN   [2]
RP   FUNCTION IN THIAMINE AND THIAMINE PYROPHOSPHATE TRANSPORT, SUBUNIT,
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=LT2;
RX   PubMed=9535878; DOI=10.1074/jbc.273.15.8946;
RA   Webb E., Claas K., Downs D.;
RT   "thiBPQ encodes an ABC transporter required for transport of thiamine and
RT   thiamine pyrophosphate in Salmonella typhimurium.";
RL   J. Biol. Chem. 273:8946-8950(1998).
CC   -!- FUNCTION: Part of the ABC transporter complex ThiBPQ involved in
CC       thiamine import (PubMed:9535878). Is also involved in thiamine
CC       pyrophosphate transport (PubMed:9535878). {ECO:0000269|PubMed:9535878}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (ThiQ),
CC       two transmembrane proteins (ThiP) and a solute-binding protein (ThiB).
CC       {ECO:0000305|PubMed:9535878}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P31550}.
CC   -!- INDUCTION: Expression is repressed by thiamine.
CC       {ECO:0000269|PubMed:9535878}.
CC   -!- DISRUPTION PHENOTYPE: Insertions in thiBPQ cause a defect in the
CC       transport of both thiamine and TPP. {ECO:0000269|PubMed:9535878}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AE006468; AAL19072.1; -; Genomic_DNA.
DR   RefSeq; NP_459113.1; NC_003197.2.
DR   RefSeq; WP_000915326.1; NC_003197.2.
DR   AlphaFoldDB; Q7CR85; -.
DR   SMR; Q7CR85; -.
DR   STRING; 99287.STM0108; -.
DR   PaxDb; Q7CR85; -.
DR   EnsemblBacteria; AAL19072; AAL19072; STM0108.
DR   GeneID; 1251626; -.
DR   KEGG; stm:STM0108; -.
DR   PATRIC; fig|99287.12.peg.111; -.
DR   HOGENOM; CLU_026974_6_0_6; -.
DR   OMA; PTTNWMY; -.
DR   PhylomeDB; Q7CR85; -.
DR   BioCyc; SENT99287:STM0108-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR   GO; GO:0030975; F:thiamine binding; IBA:GO_Central.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IBA:GO_Central.
DR   GO; GO:0015888; P:thiamine transport; IBA:GO_Central.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd13545; PBP2_TbpA; 1.
DR   InterPro; IPR006061; SBP_1_CS.
DR   InterPro; IPR005967; ThiB.
DR   InterPro; IPR005948; ThiB-like.
DR   TIGRFAMs; TIGR01254; sfuA; 1.
DR   TIGRFAMs; TIGR01276; thiB; 1.
DR   PROSITE; PS01037; SBP_BACTERIAL_1; 1.
PE   1: Evidence at protein level;
KW   Periplasm; Reference proteome; Signal; Transport.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..327
FT                   /note="Thiamine-binding periplasmic protein"
FT                   /id="PRO_5004287048"
FT   BINDING         59..60
FT                   /ligand="thiamine"
FT                   /ligand_id="ChEBI:CHEBI:18385"
FT                   /evidence="ECO:0000250|UniProtKB:P31550"
FT   BINDING         161..162
FT                   /ligand="thiamine"
FT                   /ligand_id="ChEBI:CHEBI:18385"
FT                   /evidence="ECO:0000250|UniProtKB:P31550"
FT   BINDING         197
FT                   /ligand="thiamine"
FT                   /ligand_id="ChEBI:CHEBI:18385"
FT                   /evidence="ECO:0000250|UniProtKB:P31550"
FT   BINDING         215..218
FT                   /ligand="thiamine"
FT                   /ligand_id="ChEBI:CHEBI:18385"
FT                   /evidence="ECO:0000250|UniProtKB:P31550"
SQ   SEQUENCE   327 AA;  36264 MW;  333C9A364BB162CB CRC64;
     MLKKYLPLLL LCAAPAFAKP VLTVYTYDSF AADWGPGPAV KKAFEADCNC ELKLVALEDG
     VSLLNRLRME GKNSKADVVL GLDNNLLEAA TQTKLFAKSG VANEAVKVPG GWKNDTFVPF
     DYGYFAFVYD KSKLKNPPKS LKELVESDQK WRVIYQDPRT STPGLGLLLW MRKVYGDNAP
     QAWQKLAAKT VTVTKGWSEA YGLFLKGESD LVLSYTTSPA YHIIEEKKDN YAAANFSEGH
     YLQVEVAART VASKQPELAE KFLKFMVSPA FQNAIPTGNW MYPVADVALP AGFESLAKPA
     TTLEFTPQQV AAQRQAWISE WQRAVSR