ID   THIQ_SHIF8              Reviewed;         232 AA.
AC   Q0T8D1;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=SFV_0058;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401;
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(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; CP000266; ABF02345.1; -; Genomic_DNA.
DR   RefSeq; WP_000916320.1; NC_008258.1.
DR   AlphaFoldDB; Q0T8D1; -.
DR   SMR; Q0T8D1; -.
DR   EnsemblBacteria; ABF02345; ABF02345; SFV_0058.
DR   KEGG; sfv:SFV_0058; -.
DR   HOGENOM; CLU_000604_1_22_6; -.
DR   OMA; QSIVTFP; -.
DR   BioCyc; SFLE373384:SFV_RS00335-MON; -.
DR   Proteomes; UP000000659; 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_0000274461"
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;  25051 MW;  48207B009BF68BA1 CRC64;
     MLKLTDITWL YHYLPMRFSL TVERGEQVAI LGPSGAGKST LLNLIAGFLT PASGSLTIDG
     VDHTTTPPSR RPVSMLFQEN NLFSHLTVAQ NIGLGLNPGL KLNAAQQEKM HAIARQMGID
     NLMARLPGEL SGGQRQRVAL ARCLVREQPI LLLDEPFSAL DPALRQEMLT LVSTSCQQQK
     MTLLMVSHSV EDAARIATRS VVVADGRIAW QGKTEELLSG KASASAILGI TG