ID SDPC_BACSU Reviewed; 203 AA. AC O34344; DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 16-JUN-2009, entry version 47. DE RecName: Full=Killing factor sdpC; DE AltName: Full=Toxic peptide sdpC; DE Flags: Precursor; GN Name=sdpC; Synonyms=yvaY; OrderedLocusNames=BSU33770; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168 / JH642; RA Nakamura A., Grau R., Perego M., Hoch J.A.; RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA 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., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA 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 142-169, AND INVOLVEMENT IN THE INDUCTION OF RP SDPRI. 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 FUNCTION. RC STRAIN=168 / PY79; RX PubMed=16469701; DOI=10.1016/j.cell.2005.11.041; RA Ellermeier C.D., Hobbs E.C., Gonzalez-Pastor J.E., Losick R.; RT "A three-protein signaling pathway governing immunity to a bacterial RT cannibalism toxin."; RL Cell 124:549-559(2006). 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., RA Le Breton Y.; RT "Abh and AbrB control of Bacillus subtilis antimicrobial gene RT expression."; RL J. Bacteriol. 189:7720-7732(2007). CC -!- FUNCTION: Induces the lysis of other B.subtilis cells that have CC not entered the sporulation pathway, providing a source of CC nutrients to support sporulation. Its maturation is dependent on CC sdpA and sdpB. Also functions as a ligand, being able to bind to CC sdpI thereby triggering a signal transduction cascade that CC protects the cell against the toxic effects of its own sdpC. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- INDUCTION: By spo0A during nutrient starvation, through its direct CC negative control of abrB. Repressed by abrB during regular growth CC when nutrients are plentiful, in association with the CC transcriptional repressor abh. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=I'll have you for CC supper - Issue 90 of January 2008; CC URL="http://www.expasy.org/spotlight/back_issues/sptlt090.shtml"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB006738; BAA21902.1; -; Genomic_DNA. DR EMBL; AL009126; CAB15382.1; -; Genomic_DNA. DR PIR; B70029; B70029. DR RefSeq; NP_391257.1; -. DR GeneID; 936227; -. DR GenomeReviews; AL009126_GR; BSU33770. DR KEGG; bsu:BSU33770; -. DR NMPDR; fig|224308.1.peg.3383; -. DR SubtiList; BG14076; sdpC. DR HOGENOM; O34344; -. DR BioCyc; BSUB224308:BSU3374-MON; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Secreted; Signal. FT SIGNAL 1 32 Potential. FT CHAIN 33 203 Killing factor sdpC. FT /FTId=PRO_0000013732. FT CONFLICT 161 161 Missing (in Ref. 3; AA sequence). SQ SEQUENCE 203 AA; 22221 MW; 4928C22C6AB4BEBC CRC64; MKSKLLRLLI VSMVTILVFS LVGLSKESST SAKENHTFSG EDYFRGLLFG QGEVGKLISN DLDPKLVKEA NSTEGKKLVN DVVKFIKKDQ PQYMDELKQS IDSKDPKKLI ENMTKADQLI QKYAKKNENV KYSSNKVTPS CGLYAVCVAA GYLYVVGVNA VALQTAAAVT TAVWKYVAKY SSSASNNSDL EAAAAKTLKL IHQ //