ID ECFA1_THEMA Reviewed; 259 AA. AC Q9X1Z1; DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 143. DE RecName: Full=Energy-coupling factor transporter ATP-binding protein EcfA1 {ECO:0000255|HAMAP-Rule:MF_01710}; DE Short=ECF transporter A component EcfA1 {ECO:0000255|HAMAP-Rule:MF_01710}; DE EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_01710}; GN Name=ecfA1 {ECO:0000255|HAMAP-Rule:MF_01710}; Synonyms=cbiO, ecfA'; GN OrderedLocusNames=TM_1663; OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 OS / MSB8). OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae; OC Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F., RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). RN [2] RP FUNCTION AS A TRANSPORT COMPONENT, SUBUNIT, SUBCELLULAR LOCATION, RP EXPRESSION IN E.COLI, ATP-BINDING, AND X-RAY CRYSTALLOGRAPHY (2.7 RP ANGSTROMS) OF 5-259 IN COMPLEX WITH ADP. RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8; RX PubMed=23359690; DOI=10.1073/pnas.1217361110; RA Karpowich N.K., Wang D.N.; RT "Assembly and mechanism of a group II ECF transporter."; RL Proc. Natl. Acad. Sci. U.S.A. 110:2534-2539(2013). 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 (Probable). Expression of the complex plus RibU in CC E.coli allows riboflavin uptake; uptake does not occur in the absence CC of RibU or the EcfA1A2T complex. {ECO:0000255|HAMAP-Rule:MF_01710, CC ECO:0000269|PubMed:23359690, ECO:0000305}. CC -!- SUBUNIT: Forms a heterodimer with EcfA2. Forms a stable energy-coupling CC factor (ECF) transporter complex composed of 2 membrane-embedded CC substrate-binding proteins (S component, RibU, BioY), 2 ATP-binding CC proteins (A component) and 2 transmembrane proteins (T component) upon CC coexpression in E.coli. Stable subcomplexes with both A plus T CC components can also be isolated. This complex interacts with at least 2 CC substrate-specific components, BioY and RibU. CC {ECO:0000269|PubMed:23359690}. CC -!- INTERACTION: CC Q9X1Z1; Q9WY65: ecfA2; NbExp=2; IntAct=EBI-16160756, EBI-16160779; CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000305|PubMed:23359690}; Peripheral membrane protein CC {ECO:0000305|PubMed:23359690}. CC -!- MISCELLANEOUS: Structure 4HLU is probably in the open state. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Energy-coupling CC factor EcfA family. {ECO:0000255|HAMAP-Rule:MF_01710}. 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; AE000512; AAD36730.1; -; Genomic_DNA. DR PIR; E72224; E72224. DR RefSeq; NP_229463.1; NC_000853.1. DR RefSeq; WP_004082181.1; NZ_CP011107.1. DR PDB; 4HLU; X-ray; 2.70 A; C/D=2-259. DR PDB; 4ZIR; X-ray; 3.00 A; B=2-259. DR PDBsum; 4HLU; -. DR PDBsum; 4ZIR; -. DR AlphaFoldDB; Q9X1Z1; -. DR SMR; Q9X1Z1; -. DR DIP; DIP-61611N; -. DR IntAct; Q9X1Z1; 1. DR STRING; 243274.TM_1663; -. DR TCDB; 3.A.1.25.5; the atp-binding cassette (abc) superfamily. DR PaxDb; 243274-THEMA_05930; -. DR DNASU; 897908; -. DR EnsemblBacteria; AAD36730; AAD36730; TM_1663. DR KEGG; tma:TM1663; -. DR eggNOG; COG1122; Bacteria. DR InParanoid; Q9X1Z1; -. DR OrthoDB; 9784332at2; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; IGI:UniProtKB. DR GO; GO:0032218; P:riboflavin transport; IGI:UniProtKB. DR CDD; cd03225; ABC_cobalt_CbiO_domain1; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like_ATP-bd. DR InterPro; IPR017871; ABC_transporter-like_CS. DR InterPro; IPR015856; ABC_transpr_CbiO/EcfA_su. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR43553:SF24; ENERGY-COUPLING FACTOR TRANSPORTER ATP-BINDING PROTEIN ECFA1; 1. DR PANTHER; PTHR43553; HEAVY METAL TRANSPORTER; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51246; CBIO; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Membrane; KW Nucleotide-binding; Reference proteome; Translocase; Transport. FT CHAIN 1..259 FT /note="Energy-coupling factor transporter ATP-binding FT protein EcfA1" FT /id="PRO_0000092116" FT DOMAIN 3..230 FT /note="ABC transporter" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01710" FT ACT_SITE 157 FT /note="Proton acceptor" FT /evidence="ECO:0000255" FT BINDING 38..43 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT STRAND 2..7 FT /evidence="ECO:0007829|PDB:4HLU" FT STRAND 9..18 FT /evidence="ECO:0007829|PDB:4HLU" FT STRAND 30..34 FT /evidence="ECO:0007829|PDB:4HLU" FT HELIX 41..49 FT /evidence="ECO:0007829|PDB:4HLU" FT STRAND 55..60 FT /evidence="ECO:0007829|PDB:4ZIR" FT HELIX 67..73 FT /evidence="ECO:0007829|PDB:4HLU" FT STRAND 74..77 FT /evidence="ECO:0007829|PDB:4HLU" FT STRAND 79..81 FT /evidence="ECO:0007829|PDB:4HLU" FT TURN 82..84 FT /evidence="ECO:0007829|PDB:4HLU" FT STRAND 87..89 FT /evidence="ECO:0007829|PDB:4ZIR" FT HELIX 90..95 FT /evidence="ECO:0007829|PDB:4HLU" FT STRAND 98..101 FT /evidence="ECO:0007829|PDB:4HLU" FT HELIX 108..118 FT /evidence="ECO:0007829|PDB:4HLU" FT HELIX 129..131 FT /evidence="ECO:0007829|PDB:4HLU" FT HELIX 134..146 FT /evidence="ECO:0007829|PDB:4HLU" FT STRAND 151..157 FT /evidence="ECO:0007829|PDB:4HLU" FT TURN 158..161 FT /evidence="ECO:0007829|PDB:4HLU" FT HELIX 164..178 FT /evidence="ECO:0007829|PDB:4HLU" FT TURN 179..181 FT /evidence="ECO:0007829|PDB:4HLU" FT STRAND 183..187 FT /evidence="ECO:0007829|PDB:4HLU" FT HELIX 191..193 FT /evidence="ECO:0007829|PDB:4HLU" FT STRAND 199..204 FT /evidence="ECO:0007829|PDB:4HLU" FT STRAND 207..212 FT /evidence="ECO:0007829|PDB:4HLU" FT HELIX 214..220 FT /evidence="ECO:0007829|PDB:4HLU" FT STRAND 223..225 FT /evidence="ECO:0007829|PDB:4HLU" FT HELIX 229..237 FT /evidence="ECO:0007829|PDB:4HLU" FT HELIX 242..246 FT /evidence="ECO:0007829|PDB:4ZIR" SQ SEQUENCE 259 AA; 29376 MW; 80B492FFF04A2C6A CRC64; MKITLNSVSF RYNGDYVLKD VNAEFETGKI YVVVGKNGSG KTTLLKILAG LLEAEGEIFL DGSPADPFLL RKNVGYVFQN PSSQIIGATV EEDVAFSLEI MGLDESEMRK RIKKVLELVG LSGLEKEDPL NLSGGQKQRL AIASMLARDT RFLALDEPVS MLDPPSQREI FQVLESLKNE GKGIILVTHE LEYLDDMDFI LHISNGTIDF CGSWEEFVER EFDDVEIPFK WKLWKKCGKI NLWEDRYENS GNQRRRDTV //