ID   ECFA_STRPY              Reviewed;         279 AA.
AC   P0C0E9; O87533; Q99XI1;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Energy-coupling factor transporter ATP-binding protein EcfA {ECO:0000255|HAMAP-Rule:MF_01710};
DE            Short=ECF transporter A component EcfA {ECO:0000255|HAMAP-Rule:MF_01710};
DE            EC=3.6.3.- {ECO:0000255|HAMAP-Rule:MF_01710};
GN   Name=ecfA {ECO:0000255|HAMAP-Rule:MF_01710}; Synonyms=cbiO, stpA;
OS   Streptococcus pyogenes.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=282;
RX   PubMed=9733702; DOI=10.1128/jb.180.18.4955-4959.1998;
RA   Ashbaugh C.D., Alberti S., Wessels M.R.;
RT   "Molecular analysis of the capsule gene region of group A Streptococcus:
RT   the hasAB genes are sufficient for capsule expression.";
RL   J. Bacteriol. 180:4955-4959(1998).
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=AAC61484.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF082738; AAC61484.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_002992388.1; NZ_WXZI01000010.1.
DR   RefSeq; WP_011018337.1; NZ_WVHJ01000003.1.
DR   AlphaFoldDB; P0C0E9; -.
DR   SMR; P0C0E9; -.
DR   PATRIC; fig|1314.168.peg.1021; -.
DR   eggNOG; COG1122; Bacteria.
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; 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; Hydrolase; Membrane; Nucleotide-binding;
KW   Transport.
FT   CHAIN           1..279
FT                   /note="Energy-coupling factor transporter ATP-binding
FT                   protein EcfA"
FT                   /id="PRO_0000092104"
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   279 AA;  31113 MW;  D52BA8B68FD32166 CRC64;
     MSAIIELKKV TFNYHKDQEK PTLDGVSFHV KQGEWLSIIG HNGSGKSTTI RLIDGLLEPE
     SGSIIVDGDL LTITNVWEIR HKIGMVFQNP DNQFVGATVE DDVAFGLENK GIAHEDIKER
     VNHALELVGM QNFKEKEPAR LSGGQKQRVA IAGAVAMKPK IIILDEATSM LDPKGRLELI
     KTIKNIRDDY QLTVISITHD LDEVALSDRV LVMKDGQVES TSTPEQLFAR GDELLQLGLD
     IPFTTSVVQM LQEEGYPIDY GYLTEKELEN QLCQLISKM