(data stored in SCRATCH zone)

SWISSPROT: SKFC_BACSU

ID   SKFC_BACSU              Reviewed;         496 AA.
AC   O31425; C0H3T0; O31426; Q7DL63;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 2.
DT   11-DEC-2019, entry version 84.
DE   RecName: Full=Sporulation-killing factor biosynthesis protein SkfC;
GN   Name=skfC {ECO:0000303|PubMed:12817086}; Synonyms=skfD, ybcS, ybcT;
GN   OrderedLocusNames=BSU01935; ORFNames=BSU01930, BSU01940;
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   SEQUENCE REVISION.
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   FUNCTION IN SYNTHESIS OF SKFA, 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   [5]
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: Required for production of the bacteriocin SkfA.
CC       {ECO:0000269|PubMed:12817086}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAA33090.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAA33091.1; Type=Frameshift; Evidence={ECO:0000305};
DR   EMBL; AB006424; BAA33090.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AB006424; BAA33091.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL009126; CAX52541.1; -; Genomic_DNA.
DR   PIR; F69746; F69746.
DR   PIR; G69746; G69746.
DR   RefSeq; WP_003246417.1; NZ_JNCM01000030.1.
DR   RefSeq; YP_003097671.1; NC_000964.3.
DR   STRING; 224308.BSU01935; -.
DR   PaxDb; O31425; -.
DR   PRIDE; O31425; -.
DR   EnsemblBacteria; CAX52541; CAX52541; BSU01935.
DR   GeneID; 8302931; -.
DR   KEGG; bsu:BSU01935; -.
DR   PATRIC; fig|224308.179.peg.200; -.
DR   eggNOG; ENOG41066N6; Bacteria.
DR   eggNOG; ENOG411294V; LUCA.
DR   BioCyc; BSUB:BSU01935-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0030152; P:bacteriocin biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0071586; P:CAAX-box protein processing; IEA:InterPro.
DR   InterPro; IPR003675; CAAX_protease_2.
DR   Pfam; PF02517; CPBP; 1.
PE   1: Evidence at protein level;
DR   PRODOM; O31425.
DR   SWISS-2DPAGE; O31425.
KW   Antibiotic biosynthesis; Bacteriocin biosynthesis; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..496
FT                   /note="Sporulation-killing factor biosynthesis protein
FT                   SkfC"
FT                   /id="PRO_0000013690"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        331..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        399..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        443..463
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   496 AA;  56292 MW;  2380A24F80381171 CRC64;
     MNSLSLVFWS ILAVVGLLLF IKFKPPTIAS LLLSKDEAKE ISIQFIKEFV GIDVENWDFY
     SVYWYDHDTV NKLHHLGILK KNRKVLYDVG LVESWRVRFV HQNQSFVVGV NANREITFFY
     ADVPKKTLSG KFEQVSPETL KQRLMASPDG LWSRANMTGT GKKEEDFREV STYWYIAEAG
     DIRLKVTVEL QGGRISYIGT EQEILTDQMS KVIRDEQVES TFGVSGMLGS ALAMILAILI
     LVFMDVQTSI IFSLVLGLLI IICQSLTLKE DIQLTIVNAY DARMSVKTVS LLGILSTLLT
     GLLTGFVVFI CSLAGNALAG DFGWKTFEQP IVQIFYGIGA GLISLGVTSL LFNLLEKKQY
     LRISPELSNR TVFLSGFTFR QGLNMSIQSS IGEEVIYRLL MIPVIWWMSG NILISIIVSS
     FLWAVMHQVT GYDPRWIRWL HLFIFGCFLG VLFIKFGFIC VLVAHFIHNL VLVCMPLWQF
     KLQKHMHHDQ PKHTSL
//

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