ID   THIQ_ECOL5              Reviewed;         232 AA.
AC   Q0TLS2;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 106.
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}; OrderedLocusNames=ECP_0069;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(2006).
CC   -!- FUNCTION: Part of the ABC transporter complex ThiBPQ involved in
CC       thiamine import. Responsible for energy coupling to the transport
CC       system. {ECO:0000255|HAMAP-Rule:MF_01723}.
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; CP000247; ABG68109.1; -; Genomic_DNA.
DR   RefSeq; WP_000916270.1; NC_008253.1.
DR   AlphaFoldDB; Q0TLS2; -.
DR   SMR; Q0TLS2; -.
DR   STRING; 362663.ECP_0069; -.
DR   EnsemblBacteria; ABG68109; ABG68109; ECP_0069.
DR   KEGG; ecp:ECP_0069; -.
DR   HOGENOM; CLU_000604_1_22_6; -.
DR   OMA; QSIVTFP; -.
DR   Proteomes; UP000009182; 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   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..232
FT                   /note="Thiamine import ATP-binding protein ThiQ"
FT                   /id="PRO_0000274441"
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   232 AA;  25102 MW;  DC75FEC5EE6E03B2 CRC64;
     MLKLTDITWL YHHLPMRFSL TVERGEQVAI LGPSGAGKST LLNLIAGFLT PASGLLTIDD
     VDHTTTPPSR RPVSMLFQEN NLFSHLTVAQ NIGLGLNPGL KLNAAQQKKM HAIAHQMGID
     NLMARLPGEL SGGQRQRVAL ARCLVREQPI LLLDEPFSAL DPALRQEMLT LVSTSCQQQK
     MTLLMVSHSV EDAARIATRS VVVADGRIAW QGKTDELLSG KASASALLGI KG