ID U5RTP5_9CLOT Unreviewed; 284 AA. AC U5RTP5; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 02-JUN-2021, entry version 41. DE RecName: Full=Energy-coupling factor transporter ATP-binding protein EcfA {ECO:0000256|HAMAP-Rule:MF_01710}; DE Short=ECF transporter A component EcfA {ECO:0000256|HAMAP-Rule:MF_01710}; DE EC=7.-.-.- {ECO:0000256|HAMAP-Rule:MF_01710}; GN Name=ecfA {ECO:0000256|HAMAP-Rule:MF_01710}; GN ORFNames=CAETHG_1917 {ECO:0000313|EMBL:AGY76136.1}; OS Clostridium autoethanogenum DSM 10061. OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1341692 {ECO:0000313|EMBL:AGY76136.1, ECO:0000313|Proteomes:UP000017590}; RN [1] {ECO:0000313|EMBL:AGY76136.1, ECO:0000313|Proteomes:UP000017590} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10061 {ECO:0000313|EMBL:AGY76136.1}; RX PubMed=24655715; DOI=10.1186/1754-6834-7-40; RA Brown S.D., Nagaraju S., Utturkar S., De Tissera S., Segovia S., RA Mitchell W., Land M.L., Dassanayake A., Kopke M.; RT "Comparison of single-molecule sequencing and hybrid approaches for RT finishing the genome of Clostridium autoethanogenum and analysis of CRISPR RT systems in industrial relevant Clostridia."; RL Biotechnol. Biofuels 7:40-40(2014). CC -!- FUNCTION: ATP-binding (A) component of a common energy-coupling factor CC (ECF) ABC-transporter complex. {ECO:0000256|RuleBase:RU365104}. CC -!- FUNCTION: ATP-binding (A) component of a common energy-coupling factor CC (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF CC transporter provides the energy necessary to transport a number of CC different substrates. {ECO:0000256|HAMAP-Rule:MF_01710}. CC -!- SUBUNIT: Forms a stable energy-coupling factor (ECF) transporter CC complex composed of 2 membrane-embedded substrate-binding proteins (S CC component), 2 ATP-binding proteins (A component) and 2 transmembrane CC proteins (T component). {ECO:0000256|HAMAP-Rule:MF_01710, CC ECO:0000256|RuleBase:RU365104}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01710, CC ECO:0000256|RuleBase:RU365104}; Peripheral membrane protein CC {ECO:0000256|HAMAP-Rule:MF_01710, ECO:0000256|RuleBase:RU365104}. CC Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004170}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Energy-coupling CC factor EcfA family. {ECO:0000256|HAMAP-Rule:MF_01710, CC ECO:0000256|RuleBase:RU365104}. 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; CP006763; AGY76136.1; -; Genomic_DNA. DR RefSeq; WP_013240663.1; NZ_CP012395.1. DR EnsemblBacteria; AGY76136; AGY76136; CAETHG_1917. DR KEGG; cah:CAETHG_1917; -. DR PATRIC; fig|1341692.11.peg.1939; -. DR HOGENOM; CLU_000604_1_22_9; -. DR Proteomes; UP000017590; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IEA:InterPro. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0006824; P:cobalt ion transport; IEA:InterPro. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR015856; ABC_transpr_CbiO/EcfA_su. DR InterPro; IPR005876; Co_trans_ATP-bd. DR InterPro; IPR030946; EcfA2. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01166; cbiO; 1. DR TIGRFAMs; TIGR04521; ECF_ATPase_2; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51246; CBIO; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01710}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01710, KW ECO:0000256|RuleBase:RU365104}; Hydrolase {ECO:0000313|EMBL:AGY76136.1}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01710, ECO:0000256|RuleBase:RU365104}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01710}; Reference proteome {ECO:0000313|Proteomes:UP000017590}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01710}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01710, ECO:0000256|RuleBase:RU365104}. FT DOMAIN 2..227 FT /note="CBIO" FT /evidence="ECO:0000259|PROSITE:PS51246" FT DOMAIN 3..245 FT /note="ABC transporter" FT /evidence="ECO:0000259|PROSITE:PS50893" FT NP_BIND 40..47 FT /note="ATP" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00434" SQ SEQUENCE 284 AA; 31839 MW; 01AF91074667E3E5 CRC64; MPIKIENLTH IYMKGSPFEK KALDDINIEI EDGEFVALIG HTGSGKSTLI QHINGLLKPS SGKIIVDGVD ITDKKINLNF IRKKVGLVFQ YPEYQLFEET IEKDIAFGPK NLGLSDDDIN KRVKRAMNMV GLKYEDYKDK SPFELSGGQK RRVAIAGVVA MEPKVLILDE PTAGLDPKGR DDIFSEIKNL HREYNMTIIF VSHSMEDVAK LAGRIIVMHQ GKCILDGPPE KVFNEVDTLE SVGLAVPQVT YMVKKLREKG INISKDVFTV KQAKEEILKI LNKS //