ECFA1_THEMA
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 03-AUG-2022, entry version 136.
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; Thermotogae; Thermotogales; Thermotogaceae; 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}.
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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.THEMA_05930; -.
DR TCDB; 3.A.1.25.5; the atp-binding cassette (abc) superfamily.
DR DNASU; 897908; -.
DR EnsemblBacteria; AAD36730; AAD36730; TM_1663.
DR KEGG; tma:TM1663; -.
DR eggNOG; COG1122; Bacteria.
DR InParanoid; Q9X1Z1; -.
DR OMA; YALELCP; -.
DR OrthoDB; 1713578at2; -.
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: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; -; 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 Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 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
