THIQ_VIBPA
ID THIQ_VIBPA Reviewed; 234 AA.
AC Q87SV4;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=VP0318;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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; BA000031; BAC58581.1; -; Genomic_DNA.
DR RefSeq; NP_796697.1; NC_004603.1.
DR RefSeq; WP_005454663.1; NC_004603.1.
DR AlphaFoldDB; Q87SV4; -.
DR SMR; Q87SV4; -.
DR STRING; 223926.28805301; -.
DR EnsemblBacteria; BAC58581; BAC58581; BAC58581.
DR GeneID; 1187785; -.
DR KEGG; vpa:VP0318; -.
DR PATRIC; fig|223926.6.peg.306; -.
DR eggNOG; COG3840; Bacteria.
DR HOGENOM; CLU_000604_1_22_6; -.
DR OMA; PRREEVM; -.
DR Proteomes; UP000002493; Chromosome 1.
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..234
FT /note="Thiamine import ATP-binding protein ThiQ"
FT /id="PRO_0000274467"
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 234 AA; 25969 MW; 960A0971E38D496B CRC64;
MLVLDDVQYT YQRELFRFEL SIERGQIVSL MGPSGAGKST LLALVAGFIH PDQGDIRVDG
ESIVRKEPYQ RPFSMLFQEH NLFSHLSVRD NIGLGLHPGL KLTVDQKRQV EQAAQQVGVA
EYLDRLPEHL SGGQRQRVAL ARCFVQPHPM WLLDEPFSAL DPVLREEMLS LVKKLAAERG
ITVLMVTHHL SDAKAIASHF AFVANGKVEA VGEIDALTAE HPSKTLQAFV RAAG