ID   ECFA1_CLOTE             Reviewed;         281 AA.
AC   Q890R2;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=CTC_02576;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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; AE015927; AAO37033.1; -; Genomic_DNA.
DR   RefSeq; WP_011100694.1; NC_004557.1.
DR   AlphaFoldDB; Q890R2; -.
DR   SMR; Q890R2; -.
DR   STRING; 212717.CTC_02576; -.
DR   EnsemblBacteria; AAO37033; AAO37033; CTC_02576.
DR   GeneID; 64179972; -.
DR   KEGG; ctc:CTC_02576; -.
DR   HOGENOM; CLU_000604_1_22_9; -.
DR   OMA; RMKDFDA; -.
DR   OrthoDB; 1713578at2; -.
DR   Proteomes; UP000001412; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
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; IPR030947; EcfA_1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR04520; ECF_ATPase_1; 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;
KW   Reference proteome; Translocase; Transport.
FT   CHAIN           1..281
FT                   /note="Energy-coupling factor transporter ATP-binding
FT                   protein EcfA1"
FT                   /id="PRO_0000092003"
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;  31676 MW;  12018CA2CFB900CC CRC64;
     MDSKMIECKN VVYKYEDSNE NKFIIAVDDV SFSIDKGEFV VILGRNGSGK STMAKHMNAL
     LVPTEGKVYV DKMDTLDEEN TWNIRNKAGM VFQNPDNQIV ATIVEEDVAF GPENLGVEPK
     EIRTRVENSL KRVKMFEYKK HAPHLLSGGQ KQRVAIAGVL AMMPECIVFD EPTAMLDPSG
     RKEVINTIKE LNDEYGITIV LITHYMEEAV EADRVIVMDT GKLVMEGNPR EIFSNVKAMK
     RIGLDVPQVT ELAYELKKEG ININSDILTI DEMVNELCRL K