THIQ_SALTY
ID THIQ_SALTY Reviewed; 235 AA.
AC Q8ZRV2;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Thiamine import ATP-binding protein ThiQ {ECO:0000255|HAMAP-Rule:MF_01723};
DE EC=7.6.2.15 {ECO:0000255|HAMAP-Rule:MF_01723, ECO:0000305|PubMed:9535878};
GN Name=thiQ {ECO:0000255|HAMAP-Rule:MF_01723, ECO:0000303|PubMed:9535878};
GN OrderedLocusNames=STM0106;
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, CATALYTIC
RP ACTIVITY, SUBUNIT, 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). Responsible for energy coupling to
CC the transport system (Probable). Is also involved in thiamine
CC pyrophosphate (TPP) transport (PubMed:9535878).
CC {ECO:0000269|PubMed:9535878, ECO:0000305|PubMed:9535878}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + thiamine(out) = ADP + H(+) + phosphate +
CC thiamine(in); Xref=Rhea:RHEA:29811, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18385, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.6.2.15;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01723,
CC ECO:0000305|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:0000255|HAMAP-Rule:MF_01723, ECO:0000305|PubMed:9535878}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01723, ECO:0000305}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01723, ECO:0000305}.
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 ABC transporter superfamily. Thiamine
CC importer (TC 3.A.1.19.1) family. {ECO:0000255|HAMAP-Rule:MF_01723,
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; AE006468; AAL19070.1; -; Genomic_DNA.
DR RefSeq; NP_459111.1; NC_003197.2.
DR RefSeq; WP_000915965.1; NC_003197.2.
DR AlphaFoldDB; Q8ZRV2; -.
DR SMR; Q8ZRV2; -.
DR STRING; 99287.STM0106; -.
DR PaxDb; Q8ZRV2; -.
DR EnsemblBacteria; AAL19070; AAL19070; STM0106.
DR GeneID; 1251624; -.
DR KEGG; stm:STM0106; -.
DR PATRIC; fig|99287.12.peg.109; -.
DR HOGENOM; CLU_000604_1_22_6; -.
DR OMA; QSIVTFP; -.
DR PhylomeDB; Q8ZRV2; -.
DR BioCyc; SENT99287:STM0106-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048502; F:ABC-type thiamine transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; 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; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005968; Thiamine_ABC_ThiQ.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01277; thiQ; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51288; THIQ; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..235
FT /note="Thiamine import ATP-binding protein ThiQ"
FT /id="PRO_0000274457"
FT DOMAIN 2..230
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01723"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01723"
SQ SEQUENCE 235 AA; 25571 MW; EC4C68081FA15B41 CRC64;
MLKLIDITWL YHHLPMRFTL AVERGEQVAI LGPSGAGKST LLNLIAGFLA PASGTLLIAG
DDHTLTPPSR RPVSMLFQEN NLFSHLNVQQ NIGLGLNPGL TLNASQREKR DAIAHQMGIE
SLMTRLPGEL SGGQRQRVAL ARCLVREQPV LLLDEPFSAL DPALRQEMLT LVSDICRERQ
LTLLMVSHSV EDAARIAPRS IVVADGRIAW QGKTDELLSG QASASALLGI KSHIL
