ID   ECFA2_CLONN             Reviewed;         288 AA.
AC   A0PXX8;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Energy-coupling factor transporter ATP-binding protein EcfA2 {ECO:0000255|HAMAP-Rule:MF_01710};
DE            Short=ECF transporter A component EcfA2 {ECO:0000255|HAMAP-Rule:MF_01710};
DE            EC=3.6.3.- {ECO:0000255|HAMAP-Rule:MF_01710};
GN   Name=ecfA2 {ECO:0000255|HAMAP-Rule:MF_01710}; Synonyms=cbiO2;
GN   OrderedLocusNames=NT01CX_1147;
OS   Clostridium novyi (strain NT).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=386415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NT;
RX   PubMed=17115055; DOI=10.1038/nbt1256;
RA   Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA   Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA   Zhou S.;
RT   "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT   NT.";
RL   Nat. Biotechnol. 24:1573-1580(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; CP000382; ABK60781.1; -; Genomic_DNA.
DR   RefSeq; WP_011721238.1; NC_008593.1.
DR   AlphaFoldDB; A0PXX8; -.
DR   SMR; A0PXX8; -.
DR   STRING; 386415.NT01CX_1147; -.
DR   EnsemblBacteria; ABK60781; ABK60781; NT01CX_1147.
DR   KEGG; cno:NT01CX_1147; -.
DR   PATRIC; fig|386415.7.peg.257; -.
DR   eggNOG; COG1122; Bacteria.
DR   HOGENOM; CLU_000604_1_22_9; -.
DR   OMA; PKYLFCD; -.
DR   OrthoDB; 1752365at2; -.
DR   Proteomes; UP000008220; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; 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; 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; 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; Cell membrane; Hydrolase; Membrane; Nucleotide-binding;
KW   Reference proteome; Transport.
FT   CHAIN           1..288
FT                   /note="Energy-coupling factor transporter ATP-binding
FT                   protein EcfA2"
FT                   /id="PRO_0000287931"
FT   DOMAIN          3..245
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01710"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01710"
SQ   SEQUENCE   288 AA;  32062 MW;  6DD3F646635A2570 CRC64;
     MSIEIKNLTH IYMPGSPFER KALDNVNISI EDGEFVALIG HTGSGKSTLI QHINGLLKAS
     SGNIIIDGVD ITSEKVKLSE IRKKVGLVFQ YPEYQLFEET IEKDIAFGPK NLGLNDEQVS
     KRVKKAMNIV GLDYDVYKDK SPFDLSGGQK RRVAIAGVVA MEPKVLILDE PAAGLDPKGR
     EDILEKVKQL KEEYNMTIIL VSHSMEDVAK IAERVLVMDK GRCILDGTIK EVFNEVDILE
     SVGLAVPQVT YLVRALKSKE FNIPEDIFTI EEAKNEILKL IRGANKHD