ECFA2_STAHJ
ID ECFA2_STAHJ Reviewed; 287 AA.
AC Q4L884;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 135.
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=SH0832;
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; BAE04141.1; -; Genomic_DNA.
DR RefSeq; WP_011275146.1; NC_007168.1.
DR AlphaFoldDB; Q4L884; -.
DR SMR; Q4L884; -.
DR STRING; 279808.SH0832; -.
DR EnsemblBacteria; BAE04141; BAE04141; SH0832.
DR KEGG; sha:SH0832; -.
DR eggNOG; COG1122; Bacteria.
DR HOGENOM; CLU_000604_1_22_9; -.
DR OMA; CNTVREE; -.
DR OrthoDB; 1752365at2; -.
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:0016787; F:hydrolase activity; 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; 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 Transport.
FT CHAIN 1..287
FT /note="Energy-coupling factor transporter ATP-binding
FT protein EcfA2"
FT /id="PRO_0000287988"
FT DOMAIN 3..246
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 287 AA; 33208 MW; DB5BF7BD6A6D70F8 CRC64;
MKIKFNDVTY TYQQGTPYEY KALDHINLTI EQGKYYAIVG QTGSGKSTLI QHFNGLLKPT
NGNIEHDELT IHSKTKDKFI RPIRQKVGLV FQFPESQLFE DNIEREIEFG PKNFGMNVEE
VKERAFDLLL ELGFPRNVMS LSPFQMSGGQ MRKIAIVSIL AMNPDVIVLD EPTAGLDPKS
RQQVMELFKE IQLKQNKTII LVSHDMNEVA KYAEEIIVMN DGNIIEQVTP KELFRQGSKL
EEWHIALPDI VQLQRDIEIK HGIKFKTIAL TEKEFVSMYQ EWQHHEE