(data stored in SCRATCH9089 zone)

SWISSPROT: THIQ_PASMU

ID   THIQ_PASMU              Reviewed;         225 AA.
AC   Q9CNP9;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   11-DEC-2019, entry version 121.
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=PM0378;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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}.
DR   EMBL; AE004439; AAK02462.1; -; Genomic_DNA.
DR   RefSeq; WP_005721584.1; NC_002663.1.
DR   SMR; Q9CNP9; -.
DR   PRIDE; Q9CNP9; -.
DR   EnsemblBacteria; AAK02462; AAK02462; PM0378.
DR   GeneID; 29387996; -.
DR   KEGG; pmu:PM0378; -.
DR   eggNOG; ENOG4107T0D; Bacteria.
DR   eggNOG; COG3840; LUCA.
DR   KO; K02062; -.
DR   OMA; KARFKKH; -.
DR   Proteomes; UP000000809; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0048502; F:ATPase-coupled thiamine transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_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;
DR   PRODOM; Q9CNP9.
DR   SWISS-2DPAGE; Q9CNP9.
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Translocase; Transport.
FT   CHAIN           1..225
FT                   /note="Thiamine import ATP-binding protein ThiQ"
FT                   /id="PRO_0000274448"
FT   DOMAIN          2..225
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01723"
FT   NP_BIND         32..39
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01723"
SQ   SEQUENCE   225 AA;  25229 MW;  F2854CDEE4DB46F8 CRC64;
     MINLNGVQFS YNTFTFELDL QIPAQQKVAI IGASGAGKST LLNLIAGFAL PQQGEIWLNG
     ENHSQTQPYE RPVSILFQEN NLFTHLTVAE NMALGLKPSL KLTALEQQRV QQVASAVGLQ
     GFLNQLPTQL SGGQKQRVAL ARCLLRDKPI LLLDEPFSAL DPDLRAEMLH LLLQLCDEKK
     LTLLIVTHQV NELQQKMDRM IRFEHGRMSE STILKDNFNE KQTAL
//

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