THIQ_ECOLI
ID THIQ_ECOLI Reviewed; 232 AA.
AC P31548; P75635; Q6IU29;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 170.
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};
GN Name=thiQ {ECO:0000255|HAMAP-Rule:MF_01723}; Synonyms=yabJ;
GN OrderedLocusNames=b0066, JW0065;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 156.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 51-214.
RC STRAIN=B / Bc251;
RX PubMed=12664169; DOI=10.1007/s00239-002-2423-0;
RA Lenski R.E., Winkworth C.L., Riley M.A.;
RT "Rates of DNA sequence evolution in experimental populations of Escherichia
RT coli during 20,000 generations.";
RL J. Mol. Evol. 56:498-508(2003).
RN [5]
RP FUNCTION IN THIAMINE TRANSPORT.
RC STRAIN=K12 / KG33;
RX PubMed=12175925; DOI=10.1016/s0005-2736(02)00477-7;
RA Hollenbach A.D., Dickson K.A., Washabaugh M.W.;
RT "Thiamine transport in Escherichia coli: the mechanism of inhibition by the
RT sulfhydryl-specific modifier N-ethylmaleimide.";
RL Biochim. Biophys. Acta 1564:421-428(2002).
CC -!- FUNCTION: Part of the ABC transporter complex ThiBPQ involved in
CC thiamine import (PubMed:12175925). Responsible for energy coupling to
CC the transport system (Probable). {ECO:0000269|PubMed:12175925,
CC ECO:0000305}.
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 -!- 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}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01723}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01723}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Thiamine
CC importer (TC 3.A.1.19.1) family. {ECO:0000255|HAMAP-Rule:MF_01723}.
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DR EMBL; U00096; AAC73177.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96635.2; -; Genomic_DNA.
DR EMBL; AY625120; AAT42474.1; -; Genomic_DNA.
DR PIR; B64728; B64728.
DR RefSeq; NP_414608.1; NC_000913.3.
DR RefSeq; WP_000916281.1; NZ_STEB01000010.1.
DR AlphaFoldDB; P31548; -.
DR SMR; P31548; -.
DR BioGRID; 4259729; 5.
DR ComplexPortal; CPX-4387; Thiamine ABC transporter complex.
DR IntAct; P31548; 6.
DR STRING; 511145.b0066; -.
DR TCDB; 3.A.1.19.1; the atp-binding cassette (abc) superfamily.
DR jPOST; P31548; -.
DR PaxDb; P31548; -.
DR PRIDE; P31548; -.
DR EnsemblBacteria; AAC73177; AAC73177; b0066.
DR EnsemblBacteria; BAB96635; BAB96635; BAB96635.
DR GeneID; 944785; -.
DR KEGG; ecj:JW0065; -.
DR KEGG; eco:b0066; -.
DR PATRIC; fig|1411691.4.peg.2216; -.
DR EchoBASE; EB1532; -.
DR eggNOG; COG3840; Bacteria.
DR HOGENOM; CLU_000604_1_22_6; -.
DR InParanoid; P31548; -.
DR OMA; QSIVTFP; -.
DR PhylomeDB; P31548; -.
DR BioCyc; EcoCyc:SFUC-MON; -.
DR BioCyc; MetaCyc:SFUC-MON; -.
DR PRO; PR:P31548; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0048502; F:ABC-type thiamine transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
DR GO; GO:0071934; P:thiamine transmembrane transport; IC:ComplexPortal.
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..232
FT /note="Thiamine import ATP-binding protein ThiQ"
FT /id="PRO_0000093022"
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"
FT CONFLICT 66
FT /note="M -> T (in Ref. 4; AAT42474)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="V -> A (in Ref. 4; AAT42474)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="G -> E (in Ref. 4; AAT42474)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="M -> K (in Ref. 4; AAT42474)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 232 AA; 24999 MW; 22234D38F57B7C68 CRC64;
MLKLTDITWL YHHLPMRFSL TVERGEQVAI LGPSGAGKST LLNLIAGFLT PASGSLTIDG
VDHTTMPPSR RPVSMLFQEN NLFSHLTVAQ NIGLGLNPGL KLNAVQQGKM HAIARQMGID
NLMARLPGEL SGGQRQRVAL ARCLVREQPI LLLDEPFSAL DPALRQEMLT LVSTSCQQQK
MTLLMVSHSV EDAARIATRS VVVADGRIAW QGMTNELLSG KASASALLGI TG
