ID   THIQ_PECAS              Reviewed;         236 AA.
AC   Q6D0F3;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   03-AUG-2022, entry version 114.
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=ECA3846;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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=CAG76744.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX950851; CAG76744.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011095344.1; NC_004547.2.
DR   AlphaFoldDB; Q6D0F3; -.
DR   SMR; Q6D0F3; -.
DR   STRING; 218491.ECA3846; -.
DR   EnsemblBacteria; CAG76744; CAG76744; ECA3846.
DR   KEGG; eca:ECA3846; -.
DR   PATRIC; fig|218491.5.peg.3901; -.
DR   eggNOG; COG3840; Bacteria.
DR   HOGENOM; CLU_000604_1_22_6; -.
DR   OrthoDB; 1200451at2; -.
DR   Proteomes; UP000007966; 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; Reference proteome; Translocase; Transport.
FT   CHAIN           1..236
FT                   /note="Thiamine import ATP-binding protein ThiQ"
FT                   /id="PRO_0000274437"
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   236 AA;  25943 MW;  7375ACFA975EB554 CRC64;
     MIALEKLTYF YQHLPMRFDF HVKPGERIAI LGPSGAGKST LLNLVAGFLM ADSGELRLNG
     ESHRETSPAK RPVSILFQEN NLFPHLTIGQ NIALGLHPGL RLNAAQRATL QQIADRVGLT
     DLLDRLPSQV SGGQRQRAAL ARCLVRHQPI LLLDEPFSAL DPALRQEMLD LVESVCEERK
     FTLLMVSHNL DDAMRIAKRT VLIVDGQIYY DGPTQALQDG SADAAAILGI SRSSSD