(data stored in ACNUC7421 zone)

SWISSPROT: SKFE_BACSU

ID   SKFE_BACSU              Reviewed;         239 AA.
AC   O31427; Q7DL62;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   11-DEC-2019, entry version 124.
DE   RecName: Full=SkfA peptide export ATP-binding protein SkfE;
DE            EC=7.3.2.3;
GN   Name=skfE {ECO:0000303|PubMed:12817086}; Synonyms=ybdA;
GN   OrderedLocusNames=BSU01950;
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;
RA   Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.;
RT   "Sequence analysis of the 70kb region between 17 and 23 degree of the
RT   Bacillus subtilis chromosome.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
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   POSSIBLE FUNCTION IN SKFA SYNTHESIS, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168 / PY79;
RX   PubMed=12817086; DOI=10.1126/science.1086462;
RA   Gonzalez-Pastor J.E., Hobbs E.C., Losick R.;
RT   "Cannibalism by sporulating bacteria.";
RL   Science 301:510-513(2003).
RN   [4]
RP   REPRESSION BY ABRB AND ABH.
RX   PubMed=17720793; DOI=10.1128/jb.01081-07;
RA   Strauch M.A., Bobay B.G., Cavanagh J., Yao F., Wilson A., Le Breton Y.;
RT   "Abh and AbrB control of Bacillus subtilis antimicrobial gene expression.";
RL   J. Bacteriol. 189:7720-7732(2007).
CC   -!- FUNCTION: Probably part of the ABC transporter SkfEF involved in the
CC       export of the bacteriocin SKF. Probably responsible for energy coupling
CC       to the transport system. {ECO:0000305|PubMed:12817086}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + sulfate(out) = ADP + H(+) + phosphate +
CC         sulfate(in); Xref=Rhea:RHEA:10192, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.3.2.3;
CC         Evidence={ECO:0000305};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + thiosulfate(out) = ADP + H(+) + phosphate +
CC         thiosulfate(in); Xref=Rhea:RHEA:29871, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33542,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.3.2.3;
CC         Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- INDUCTION: By Spo0A (PubMed:12817086) and PhoP, during nutrient
CC       starvation, especially phosphate starvation. Repressed by AbrB during
CC       normal growth when nutrients are plentiful, in association with the
CC       transcriptional repressor Abh. {ECO:0000269|PubMed:12817086,
CC       ECO:0000269|PubMed:17720793}.
CC   -!- DISRUPTION PHENOTYPE: When the skfA-skfB-skfC-skfE-skfF-skfG-skfH
CC       operon is deleted, increased rate of spore formation; a double operon
CC       deletion (sdpA-sdpC plus skfA-skfH) makes spores even faster
CC       (PubMed:12817086). {ECO:0000269|PubMed:12817086}.
CC   -!- MISCELLANEOUS: Accelerated cannibalism by skf- cells is seen on solid
CC       media but not in liquid media. {ECO:0000269|PubMed:12817086}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. SkfA peptide
CC       export (TC 3.A.1.128.1) family. {ECO:0000305}.
DR   EMBL; AB006424; BAA33092.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11989.1; -; Genomic_DNA.
DR   PIR; H69746; H69746.
DR   RefSeq; NP_388077.1; NC_000964.3.
DR   RefSeq; WP_003234899.1; NZ_JNCM01000030.1.
DR   SMR; O31427; -.
DR   STRING; 224308.BSU01950; -.
DR   TCDB; 3.A.1.128.1; the atp-binding cassette (abc) superfamily.
DR   PaxDb; O31427; -.
DR   PRIDE; O31427; -.
DR   EnsemblBacteria; CAB11989; CAB11989; BSU01950.
DR   GeneID; 938498; -.
DR   KEGG; bsu:BSU01950; -.
DR   PATRIC; fig|224308.179.peg.201; -.
DR   eggNOG; ENOG4108WUZ; Bacteria.
DR   eggNOG; COG1131; LUCA.
DR   InParanoid; O31427; -.
DR   KO; K01990; -.
DR   PhylomeDB; O31427; -.
DR   BioCyc; BSUB:BSU01950-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0102025; F:ATPase-coupled thiosulfate transmembrane transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0030152; P:bacteriocin biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; O31427.
DR   SWISS-2DPAGE; O31427.
KW   Antibiotic biosynthesis; ATP-binding; Bacteriocin biosynthesis;
KW   Cell membrane; Membrane; Nucleotide-binding; Reference proteome;
KW   Translocase; Transport.
FT   CHAIN           1..239
FT                   /note="SkfA peptide export ATP-binding protein SkfE"
FT                   /id="PRO_0000312739"
FT   DOMAIN          4..232
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   NP_BIND         36..43
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   239 AA;  26894 MW;  1E7DFF09DFA3948A CRC64;
     MQLMQVQNLS KCYRNGDGVE HLSFSIQRGE IVALLGPNGA GKTTTIRCLT GLYKPDKGDI
     LIEGSPPGDI NVQKKVALIP DQPYLYPALT AAEHIQFRAR GYHPGKKDVK ERVYHALKEV
     HLEEKANQLC GQLSRGQKQR VVLAGAIVQD ALLYILDEPT VGLDIPSKQW LSNWLKTKTD
     QGCSAFVSTH SLEFVIETAD RVILIRDGKL MQDLYVPQFE EQAEWRKEVI RLLGEWSDE
//

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