ID   ECFA1_STAHJ             Reviewed;         270 AA.
AC   Q4L885;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 134.
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=SH0831;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE04140.1; -; Genomic_DNA.
DR   RefSeq; WP_011275145.1; NC_007168.1.
DR   AlphaFoldDB; Q4L885; -.
DR   SMR; Q4L885; -.
DR   STRING; 279808.SH0831; -.
DR   EnsemblBacteria; BAE04140; BAE04140; SH0831.
DR   GeneID; 58062987; -.
DR   KEGG; sha:SH0831; -.
DR   eggNOG; COG1122; Bacteria.
DR   HOGENOM; CLU_000604_1_22_9; -.
DR   OMA; RMKDFDA; -.
DR   OrthoDB; 1713578at2; -.
DR   Proteomes; UP000000543; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProt.
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; Translocase;
KW   Transport.
FT   CHAIN           1..270
FT                   /note="Energy-coupling factor transporter ATP-binding
FT                   protein EcfA1"
FT                   /id="PRO_0000287987"
FT   DOMAIN          9..243
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01710"
FT   BINDING         43..50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01710"
SQ   SEQUENCE   270 AA;  29679 MW;  4D6A960F94FDAA1D CRC64;
     MEANNTNIIE LKQVDFQYQG DAAFTLNNVS FKIPKNQWTS IVGHNGSGKS TIAKLIVGIE
     IATNGTIIFN QSPISNNDFK DIREHVGIVF QNPENQFVGS IVKYDVAFGL ENHAVPTEKM
     KEIVAQSISD VGMTDYADSE PHSLSGGQKQ RVAIAGVLAL SPSVIILDEA TSMLDPQAKK
     SLMSLIQEVK ATKDVTIISI THDLTEALEG DHVIVMNQGT VYKEGNPQTI FKDIKMLQEI
     GLDLPFSMKI NQLLGFDDHF ITYEGLVEKL