THIQ_RHILO
ID THIQ_RHILO Reviewed; 253 AA.
AC Q98FA5;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=mll3864;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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; BA000012; BAB50662.1; -; Genomic_DNA.
DR AlphaFoldDB; Q98FA5; -.
DR SMR; Q98FA5; -.
DR STRING; 266835.14024057; -.
DR EnsemblBacteria; BAB50662; BAB50662; BAB50662.
DR KEGG; mlo:mll3864; -.
DR eggNOG; COG3840; Bacteria.
DR HOGENOM; CLU_000604_1_22_5; -.
DR OMA; HPPVYAP; -.
DR Proteomes; UP000000552; 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..253
FT /note="Thiamine import ATP-binding protein ThiQ"
FT /id="PRO_0000274451"
FT DOMAIN 8..236
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01723"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01723"
SQ SEQUENCE 253 AA; 26616 MW; B5EC5E69C817F2D0 CRC64;
MRGKGVPVRL DKVSFSYGEA PLTFDVAFAA AEITAIMGPS GSGKSTLLNL VAGFETPQSG
GVLIGGVDVG AAPPAARPVS MVFQENNLFA HLSVEQNVGL GRSPSLRLTE VDREAIDGAL
ARTGLGGKEK RLPRELSGGE RQRVALARVL VRDRPVLLLD EPFASLGPAL RDDMLDLVAG
VHAERGMTVL FVTHQPQDAR RIGRNVVFLD NGTVAATGSA DDFFAGAGPE AFRRYIGASA
GNAVSQDIAR KRT