ID   ECFA1_STAA8             Reviewed;         269 AA.
AC   Q2FW34;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=SAOUHSC_02483;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (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; CP000253; ABD31502.1; -; Genomic_DNA.
DR   RefSeq; WP_000389662.1; NZ_LS483365.1.
DR   RefSeq; YP_500951.1; NC_007795.1.
DR   AlphaFoldDB; Q2FW34; -.
DR   SMR; Q2FW34; -.
DR   STRING; 1280.SAXN108_2472; -.
DR   EnsemblBacteria; ABD31502; ABD31502; SAOUHSC_02483.
DR   GeneID; 3920860; -.
DR   KEGG; sao:SAOUHSC_02483; -.
DR   PATRIC; fig|93061.5.peg.2239; -.
DR   eggNOG; COG1122; Bacteria.
DR   HOGENOM; CLU_000604_1_22_9; -.
DR   OMA; RMKDFDA; -.
DR   PRO; PR:Q2FW34; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
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..269
FT                   /note="Energy-coupling factor transporter ATP-binding
FT                   protein EcfA1"
FT                   /id="PRO_0000287984"
FT   DOMAIN          8..242
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01710"
FT   BINDING         42..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01710"
SQ   SEQUENCE   269 AA;  30050 MW;  949E97384B921FD7 CRC64;
     MEDKNSVIVF KNVSFQYQSD ASFTLKDVSF NIPKGQWTSI VGHNGSGKST IAKLMIGIEK
     VKSGEIFYNN QAITDDNFEK LRKDIGIVFQ NPDNQFVGSI VKYDVAFGLE NHAVPYDEMH
     RRVSEALKQV DMLERADYEP NALSGGQKQR VAIASVLALN PSVIILDEAT SMLDPDARQN
     LLDLVRKVKS EHNITIISIT HDLSEAMEAD HVIVMNKGTV YKEGTATEIF DNAEELTRIG
     LDLPFPIKIN QMLGHQTSFL TYEGLVDQL