ECFA1_BACSU
ID ECFA1_BACSU Reviewed; 281 AA.
AC P40735;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Energy-coupling factor transporter ATP-binding protein EcfA1 {ECO:0000255|HAMAP-Rule:MF_01710};
DE Short=ECF transporter A component EcfA {ECO:0000255|HAMAP-Rule:MF_01710};
DE EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_01710};
GN Name=ecfA {ECO:0000255|HAMAP-Rule:MF_01710}; Synonyms=cbiO1, ybaD, ybxA;
GN OrderedLocusNames=BSU01450;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969501; DOI=10.1099/13500872-142-11-3039;
RA Yasumoto K., Liu H., Jeong S.M., Ohashi Y., Kakinuma S., Tanaka K.,
RA Kawamura F., Yoshikawa H., Takahashi H.;
RT "Sequence analysis of a 50 kb region between spo0H and rrnH on the Bacillus
RT subtilis chromosome.";
RL Microbiology 142:3039-3046(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 97; 235 AND 279.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
RX PubMed=2496109; DOI=10.1128/jb.171.5.2553-2562.1989;
RA Boylan S.A., Suh J.-W., Thomas S.M., Price C.W.;
RT "Gene encoding the alpha core subunit of Bacillus subtilis RNA polymerase
RT is cotranscribed with the genes for initiation factor 1 and ribosomal
RT proteins B, S13, S11, and L17.";
RL J. Bacteriol. 171:2553-2562(1989).
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; D64126; BAA10983.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11921.2; -; Genomic_DNA.
DR EMBL; M26414; AAA22219.1; -; Genomic_DNA.
DR PIR; E69751; E69751.
DR RefSeq; NP_388026.2; NC_000964.3.
DR RefSeq; WP_004399689.1; NZ_JNCM01000029.1.
DR AlphaFoldDB; P40735; -.
DR SMR; P40735; -.
DR STRING; 224308.BSU01450; -.
DR PaxDb; P40735; -.
DR PRIDE; P40735; -.
DR EnsemblBacteria; CAB11921; CAB11921; BSU_01450.
DR GeneID; 938925; -.
DR KEGG; bsu:BSU01450; -.
DR PATRIC; fig|224308.179.peg.149; -.
DR eggNOG; COG1122; Bacteria.
DR InParanoid; P40735; -.
DR OMA; RMKDFDA; -.
DR PhylomeDB; P40735; -.
DR BioCyc; BSUB:BSU01450-MON; -.
DR Proteomes; UP000001570; 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..281
FT /note="Energy-coupling factor transporter ATP-binding
FT protein EcfA1"
FT /id="PRO_0000091986"
FT DOMAIN 7..242
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01710"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01710"
FT CONFLICT 97
FT /note="V -> F (in Ref. 1; BAA10983)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="E -> G (in Ref. 1; BAA10983)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="S -> L (in Ref. 1; BAA10983)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 281 AA; 31459 MW; E17C41502850F43C CRC64;
MNQNQLISVE DIVFRYRKDA ERRALDGVSL QVYEGEWLAI VGHNGSGKST LARALNGLIL
PESGDIEVAG IQLTEESVWE VRKKIGMVFQ NPDNQFVGTT VRDDVAFGLE NNGVPREEMI
ERVDWAVKQV NMQDFLDQEP HHLSGGQKQR VAIAGVIAAR PDIIILDEAT SMLDPIGREE
VLETVRHLKE QGMATVISIT HDLNEAAKAD RIIVMNGGKK YAEGPPEEIF KLNKELVRIG
LDLPFSFQLS QLLRENGLAL EENHLTQEGL VKELWTLQSK M
