ID ECFA1_CLOPS Reviewed; 281 AA.
AC Q0SQH5;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 88.
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=cbiO1;
GN OrderedLocusNames=CPR_2368;
OS Clostridium perfringens (strain SM101 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=289380;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM101 / Type A;
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
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:0000255|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:0000255|HAMAP-Rule:MF_01710}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01710};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01710}.
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; CP000312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q0SQH5; -.
DR SMR; Q0SQH5; -.
DR Proteomes; UP000001824; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProt.
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; IPR030947; EcfA_1.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR04520; ECF_ATPase_1; 1.
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 3: Inferred from homology;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding; Translocase;
KW Transport.
FT CHAIN 1..281
FT /note="Energy-coupling factor transporter ATP-binding
FT protein EcfA1"
FT /id="PRO_0000287936"
FT DOMAIN 6..245
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01710"
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01710"
SQ SEQUENCE 281 AA; 31381 MW; 5960C39B6CBB6398 CRC64;
MGENMIKSED LVFKYVNSEE QNEKLAINHV SMEVKNGEFL VILGHNGSGK STMAKHMNAL
LLPSGGKMYV DGLDTSDIEN IWEVRRRAGM VFQNPDNQLV ATIVEEDVAF GPENLGVDPK
EIRERVDDSL KAVGMYEYRK HAPHLLSGGQ KQRIAIAGIL AMRPKCIVLD EPTAMLDPSG
RNEVMKTIKE VNKKFGITII LITHYMDEAA QADRIIVMDK GEKVMEGVPR EIFSQVKKIK
SIGLDVPQVT ELAYELQKEG VDISTEILNI DEMVNALCQL K
//
