ID I4T5S8_ECOLX Unreviewed; 232 AA. AC I4T5S8; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 29-OCT-2014, entry version 12. DE RecName: Full=Thiamine import ATP-binding protein ThiQ {ECO:0000256|HAMAP-Rule:MF_01723}; DE EC=3.6.3.- {ECO:0000256|HAMAP-Rule:MF_01723}; GN Name=thiQ {ECO:0000256|HAMAP-Rule:MF_01723, GN ECO:0000313|EMBL:EIL58069.1}; GN ORFNames=EC54115_03177 {ECO:0000313|EMBL:EIL58069.1}; OS Escherichia coli 541-15. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=752785 {ECO:0000313|EMBL:EIL58069.1}; RN [1] {ECO:0000313|EMBL:EIL58069.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=541-15 {ECO:0000313|EMBL:EIL58069.1}; RA Suzuki H., Richards V., Lefebure T., Pavinski Bitar P., Lang P., RA Stanhope M.; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Part of the ABC transporter complex ThiBPQ involved in CC thiamine import. Responsible for energy coupling to the transport CC system. {ECO:0000256|HAMAP-Rule:MF_01723}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (ThiQ), two transmembrane proteins (ThiP) and a solute-binding CC protein (ThiB). {ECO:0000256|HAMAP-Rule:MF_01723}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_01723}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01723}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000256|RuleBase:RU000684}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Thiamine CC importer (TC 3.A.1.19.1) family. {ECO:0000256|HAMAP- CC Rule:MF_01723}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000256|HAMAP- CC Rule:MF_01723}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIL58069.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJWQ01000027; EIL58069.1; -; Genomic_DNA. DR EnsemblBacteria; EIL58069; EIL58069; EC54115_03177. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0048502; F:thiamine-transporting ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0015888; P:thiamine transport; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. 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; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01723, KW ECO:0000256|RuleBase:RU000684}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01723}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01723}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01723}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01723, KW ECO:0000256|RuleBase:RU000684}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01723}. FT DOMAIN 2 230 ABC transporter. {ECO:0000256|HAMAP-Rule: FT MF_01723}. FT NP_BIND 32 39 ATP. {ECO:0000256|HAMAP-Rule:MF_01723}. SQ SEQUENCE 232 AA; 25064 MW; 82ACE8F0D1AA4313 CRC64; MLKLTDITWL YHHLPMRFSL TVERGEQVAI LGPSGAGKST LLNLIAGFLT PASGSLTIDS VDHTTTPPSR RPVSMLFQEN NLFSHLTVAQ NIGLGLNPGL KLNAAQQEKM HAIARQMGID NLMARLPGEL SGGQRQRVAL ARCLVREQPI LLLDEPFSAL DPALRHEMLT LVSTSCQQQK MTLLMVSHSV EDAARIATRS VVVADGRIAW QGKTEELLSG KASASAILGI TG //