(data stored in SCRATCH zone)

SWISSPROT: SKFA_BACSU

ID   SKFA_BACSU              Reviewed;          55 AA.
AC   O31422;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   11-DEC-2019, entry version 80.
DE   RecName: Full=Sporulation killing factor {ECO:0000303|PubMed:20805502};
DE            Short=SKF {ECO:0000303|PubMed:20805502};
DE   AltName: Full=Sporulation-killing factor SkfA;
DE   Flags: Precursor;
GN   Name=skfA {ECO:0000303|PubMed:12817086}; Synonyms=ybcO;
GN   OrderedLocusNames=BSU01910;
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   PROTEIN SEQUENCE OF 30-55, FUNCTION, IDENTIFICATION OF ACTIVE PEPTIDE,
RP   SUBCELLULAR LOCATION, MASS SPECTROMETRY, DISULFIDE BOND, THIOETHER BOND,
RP   CROSS-LINK, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168 / PY79;
RX   PubMed=20805502; DOI=10.1073/pnas.1008368107;
RA   Liu W.T., Yang Y.L., Xu Y., Lamsa A., Haste N.M., Yang J.Y., Ng J.,
RA   Gonzalez D., Ellermeier C.D., Straight P.D., Pevzner P.A., Pogliano J.,
RA   Nizet V., Pogliano K., Dorrestein P.C.;
RT   "Imaging mass spectrometry of intraspecies metabolic exchange revealed the
RT   cannibalistic factors of Bacillus subtilis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:16286-16290(2010).
RN   [4]
RP   INHIBITION OF XANTHOMONAS GROWTH.
RC   STRAIN=168 / SO113;
RX   PubMed=11851812; DOI=10.1046/j.1365-2672.2001.01475.x;
RA   Lin D., Qu L.-J., Gu H., Chen Z.;
RT   "A 3.1-kb genomic fragment of Bacillus subtilis encodes the protein
RT   inhibiting growth of Xanthomonas oryzae pv. oryzae.";
RL   J. Appl. Microbiol. 91:1044-1050(2001).
RN   [5]
RP   FUNCTION, 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   [6]
RP   ROLE IN LIPASE PRODUCTION.
RC   STRAIN=168;
RX   PubMed=15812018; DOI=10.1128/aem.71.4.1899-1908.2005;
RA   Westers H., Braun P.G., Westers L., Antelmann H., Hecker M.,
RA   Jongbloed J.D.H., Yoshikawa H., Tanaka T., van Dijl J.M., Quax W.J.;
RT   "Genes involved in SkfA killing factor production protect a Bacillus
RT   subtilis lipase against proteolysis.";
RL   Appl. Environ. Microbiol. 71:1899-1908(2005).
RN   [7]
RP   REPRESSION BY ABRB.
RX   PubMed=15687200; DOI=10.1128/jb.187.4.1357-1368.2005;
RA   Fujita M., Gonzalez-Pastor J.E., Losick R.;
RT   "High- and low-threshold genes in the Spo0A regulon of Bacillus subtilis.";
RL   J. Bacteriol. 187:1357-1368(2005).
RN   [8]
RP   INDUCTION BY PHOSPHATE STARVATION.
RC   STRAIN=168;
RX   PubMed=16816204; DOI=10.1128/jb.00084-06;
RA   Allenby N.E.E., Watts C.A., Homuth G., Pragai Z., Wipat A., Ward A.C.,
RA   Harwood C.R.;
RT   "Phosphate starvation induces the sporulation killing factor of Bacillus
RT   subtilis.";
RL   J. Bacteriol. 188:5299-5303(2006).
RN   [9]
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).
RN   [10]
RP   CROSS-LINK, AND MUTAGENESIS OF 1-MET--GLY-29; 33-CYS--MET-41; CYS-33 AND
RP   MET-41.
RC   STRAIN=168;
RX   PubMed=23282011; DOI=10.1021/ja310542g;
RA   Fluehe L., Burghaus O., Wieckowski B.M., Giessen T.W., Linne U.,
RA   Marahiel M.A.;
RT   "Two [4Fe-4S] clusters containing radical SAM enzyme SkfB catalyze
RT   thioether bond formation during the maturation of the sporulation killing
RT   factor.";
RL   J. Am. Chem. Soc. 135:959-962(2013).
CC   -!- FUNCTION: Produces a 26-residue extracellular sporulation filling
CC       factor (SKF) that induces the lysis of other B.subtilis cells that have
CC       not entered the sporulation pathway, providing a source of nutrients to
CC       support sporulation, and at the same time delaying commitment to the
CC       energetically expensive and irreversible onset of sporulation
CC       (PubMed:12817086, PubMed:20805502). Can also inhibit growth of other
CC       bacteria at high concentrations (PubMed:11851812). Addition of SKF to
CC       solid cultures induces killing, but it is much less effective than SDP
CC       (AC O34344) (PubMed:20805502). Has a role in protecting the secreted
CC       lipase LipA against proteolysis, either by modulating its folding or by
CC       acting as a protease inhibitor (PubMed:15812018).
CC       {ECO:0000269|PubMed:11851812, ECO:0000269|PubMed:12817086,
CC       ECO:0000269|PubMed:15812018, ECO:0000269|PubMed:20805502}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20805502}.
CC       Note=Probably secreted by the ABC transporter SkfEF. {ECO:0000305}.
CC   -!- INDUCTION: By Spo0A (PubMed:12817086) and PhoP (PubMed:16816204),
CC       during nutrient starvation, especially phosphate starvation. Repressed
CC       by AbrB during normal growth when nutrients are plentiful, in
CC       association with the transcriptional repressor Abh.
CC       {ECO:0000269|PubMed:12817086, ECO:0000269|PubMed:15687200,
CC       ECO:0000269|PubMed:16816204, ECO:0000269|PubMed:17720793}.
CC   -!- PTM: This is a cyclic peptide (PubMed:20805502, PubMed:23282011). The
CC       first step in SKF maturation is probably thioether bond formation
CC       (PubMed:23282011). {ECO:0000269|PubMed:20805502,
CC       ECO:0000269|PubMed:23282011}.
CC   -!- MASS SPECTROMETRY: Mass=2781.302; Method=MALDI; Note=Cyclic, disulfide-
CC       containing sactipeptide with a thioether cross-link of cysteine to
CC       methionine.; Evidence={ECO:0000269|PubMed:20805502};
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). In a single gene deletion no SKP is produced
CC       (PubMed:20805502). {ECO:0000269|PubMed:12817086,
CC       ECO:0000269|PubMed:20805502}.
CC   -!- MISCELLANEOUS: Accelerated cannibalism by skf- cells is seen on solid
CC       media but not in liquid media. {ECO:0000269|PubMed:12817086}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=I'll have you for supper
CC       - Issue 90 of January 2008;
CC       URL="https://web.expasy.org/spotlight/back_issues/090";
DR   EMBL; AB006424; BAA33086.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11984.1; -; Genomic_DNA.
DR   PIR; C69746; C69746.
DR   RefSeq; NP_388072.1; NC_000964.3.
DR   RefSeq; WP_009966416.1; NZ_JNCM01000030.1.
DR   STRING; 224308.BSU01910; -.
DR   PaxDb; O31422; -.
DR   PRIDE; O31422; -.
DR   EnsemblBacteria; CAB11984; CAB11984; BSU01910.
DR   GeneID; 938506; -.
DR   KEGG; bsu:BSU01910; -.
DR   PATRIC; fig|224308.179.peg.198; -.
DR   BioCyc; BSUB:BSU01910-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR030919; RiPP_SkfA.
DR   TIGRFAMs; TIGR04404; RiPP_SkfA; 1.
PE   1: Evidence at protein level;
DR   PRODOM; O31422.
DR   SWISS-2DPAGE; O31422.
KW   Antibiotic; Antimicrobial; Bacteriocin; Direct protein sequencing;
KW   Disulfide bond; Reference proteome; Secreted; Thioether bond.
FT   PROPEP          1..29
FT                   /evidence="ECO:0000269|PubMed:20805502"
FT                   /id="PRO_0000435140"
FT   PEPTIDE         30..55
FT                   /note="Sporulation killing factor"
FT                   /evidence="ECO:0000269|PubMed:20805502"
FT                   /id="PRO_0000049459"
FT   DISULFID        30..45
FT                   /evidence="ECO:0000269|PubMed:20805502"
FT   CROSSLNK        30..55
FT                   /note="Cyclopeptide (Cys-Ile)"
FT                   /evidence="ECO:0000269|PubMed:20805502"
FT   CROSSLNK        33..41
FT                   /note="2-(S-cysteinyl)-methionine (Cys-Met)"
FT                   /evidence="ECO:0000269|PubMed:20805502,
FT                   ECO:0000269|PubMed:23282011"
FT   MUTAGEN         1..29
FT                   /note="Missing: Cys-Met cross-link not made."
FT                   /evidence="ECO:0000269|PubMed:23282011"
FT   MUTAGEN         33..41
FT                   /note="CWASKSIAM->MWASKSIAC: Cys-Met cross-link not made,
FT                   suggests relative amino acid positions are important for
FT                   thioether bond formation."
FT                   /evidence="ECO:0000269|PubMed:23282011"
FT   MUTAGEN         33
FT                   /note="C->A,S: Cys-thioether cross-link not made."
FT                   /evidence="ECO:0000269|PubMed:23282011"
FT   MUTAGEN         41
FT                   /note="M->A,F,L,Y: Approximately wild-type amounts of Cys-
FT                   thioether cross-link made."
FT                   /evidence="ECO:0000269|PubMed:23282011"
FT   MUTAGEN         41
FT                   /note="M->E,K,Q: Cys-thioether cross-link not made."
FT                   /evidence="ECO:0000269|PubMed:23282011"
FT   MUTAGEN         41
FT                   /note="M->N,S,T: 50% wild-type amount of Cys-thioether
FT                   cross-link made."
FT                   /evidence="ECO:0000269|PubMed:23282011"
SQ   SEQUENCE   55 AA;  5934 MW;  F169E627ADBEBB55 CRC64;
     MKRNQKEWES VSKKGLMKPG GTSIVKAAGC MGCWASKSIA MTRVCALPHP AMRAI
//

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