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 03-AUG-2022, entry version 91.
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};
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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 AlphaFoldDB; O31425; -.
DR STRING; 224308.BSU01935; -.
DR PaxDb; O31425; -.
DR PRIDE; O31425; -.
DR EnsemblBacteria; CAX52541; CAX52541; BSU_01935.
DR GeneID; 8302931; -.
DR KEGG; bsu:BSU01935; -.
DR PATRIC; fig|224308.179.peg.200; -.
DR eggNOG; COG1266; Bacteria.
DR BioCyc; BSUB:BSU01935-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase 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; Rce1-like.
DR Pfam; PF02517; Rce1-like; 1.
PE 1: Evidence at protein level;
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
