ECFA1_STRSV
ID ECFA1_STRSV Reviewed; 278 AA.
AC A3CRB9;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 98.
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=SSA_2367;
OS Streptococcus sanguinis (strain SK36).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=388919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK36;
RX PubMed=17277061; DOI=10.1128/jb.01808-06;
RA Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S., Manque P.,
RA Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y., Chaplin M.D., Akan D.,
RA Paik S., Peterson D.L., Macrina F.L., Buck G.A.;
RT "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL J. Bacteriol. 189:3166-3175(2007).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABN45724.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000387; ABN45724.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_001036274.1; NC_009009.1.
DR AlphaFoldDB; A3CRB9; -.
DR SMR; A3CRB9; -.
DR STRING; 388919.SSA_2367; -.
DR EnsemblBacteria; ABN45724; ABN45724; SSA_2367.
DR KEGG; ssa:SSA_2367; -.
DR PATRIC; fig|388919.9.peg.2248; -.
DR eggNOG; COG1122; Bacteria.
DR HOGENOM; CLU_000604_1_22_9; -.
DR OrthoDB; 1713578at2; -.
DR Proteomes; UP000002148; 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;
KW Reference proteome; Translocase; Transport.
FT CHAIN 1..278
FT /note="Energy-coupling factor transporter ATP-binding
FT protein EcfA1"
FT /id="PRO_0000288008"
FT DOMAIN 5..240
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 278 AA; 31181 MW; BA60AEBED3C6FA66 CRC64;
MENIIEVRNL KYKYDSESEN YTLNDVSFQV KKGEWLSIVG HNGSGKSTTV RLIDGLLEAE
SGDIIISGDK LTAENVWEKR RQIGMVFQNP DNQFVGATVE DDVAFGLENQ GLDYDLMVER
VQQALELVGM QDFKEREPAR LSGGQKQRVA VAGVVALRPD IIILDEATSM LDPEGRLDLI
QTVKKIKDSN QLTVISITHD LDEIALSDRV LVMKEGQVES TATPRELFSR EDLEELGLDQ
PFVNQVKVAL RQSGLSLPDS YLTEKELQDQ LWALLSKM