THIQ_ECOUT
ID THIQ_ECOUT Reviewed; 232 AA.
AC Q1RGD0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 105.
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=UTI89_C0074;
OS Escherichia coli (strain UTI89 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=364106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTI89 / UPEC;
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA Gordon J.I.;
RT "Identification of genes subject to positive selection in uropathogenic
RT strains of Escherichia coli: a comparative genomics approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABE05584.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000243; ABE05584.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000916269.1; NC_007946.1.
DR AlphaFoldDB; Q1RGD0; -.
DR SMR; Q1RGD0; -.
DR EnsemblBacteria; ABE05584; ABE05584; UTI89_C0074.
DR KEGG; eci:UTI89_C0074; -.
DR HOGENOM; CLU_000604_1_22_6; -.
DR OMA; QSIVTFP; -.
DR Proteomes; UP000001952; 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_0000274438"
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; 25088 MW; DC75F9C2EE6904B2 CRC64;
MLKLTDITWL YHHLPMRFSL TVERGEQVAI LGPSGAGKST LLNLIAGFLT PASGLLTIDD
VDHTTTPPSR RPVSMLFQEN NLFSHLTVAQ NIGLGLNPGL KLNAAQQKKM HAIAHQMGID
NLMARLPGEL SGGQRQRVAL ARCLVREQPI LLLDEPFSAL DPALRQEMLT LVSSSCQQQK
MTLLMVSHSV EDAARIATRS VVVADGRIAW QGKTDELLSG KASASALLGI KG