(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, 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 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}.
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   SMR; P40735; -.
DR   STRING; 224308.BSU01450; -.
DR   PaxDb; P40735; -.
DR   PRIDE; P40735; -.
DR   EnsemblBacteria; CAB11921; CAB11921; BSU01450.
DR   GeneID; 938925; -.
DR   KEGG; bsu:BSU01450; -.
DR   PATRIC; fig|224308.179.peg.149; -.
DR   eggNOG; ENOG4108JJB; Bacteria.
DR   eggNOG; COG1122; LUCA.
DR   InParanoid; P40735; -.
DR   KO; K16786; -.
DR   OMA; FGVLFQK; -.
DR   PhylomeDB; P40735; -.
DR   BioCyc; BSUB:BSU01450-MONOMER; -.
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:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_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;
DR   PRODOM; P40735.
DR   SWISS-2DPAGE; P40735.
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   NP_BIND         42..49
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01710"
FT   ACT_SITE        168
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
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
//

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