SDPC_BACSU
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 03-AUG-2022, entry version 97.
DE RecName: Full=Sporulation delaying protein C {ECO:0000303|PubMed:20805502};
DE Short=SdpC;
DE AltName: Full=Cannibalism toxin SDP {ECO:0000303|PubMed:22469514};
DE AltName: Full=Killing factor SdpC;
DE AltName: Full=Toxic peptide SdpC;
DE Contains:
DE RecName: Full=Sporulation delaying protein {ECO:0000303|PubMed:20805502};
DE Short=SDP {ECO:0000303|PubMed:20805502};
DE Flags: Precursor;
GN Name=sdpC {ECO:0000303|PubMed:12817086}; Synonyms=yvaY;
GN OrderedLocusNames=BSU33770;
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 / 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 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 33-42, AND SUBUNIT.
RC STRAIN=168 / DB104;
RX PubMed=10816431; DOI=10.1042/bj3480367;
RA Mueller J.P., Ozegowski J., Vettermann S., Swaving J., Van Wely K.H.,
RA Driessen A.J.;
RT "Interaction of Bacillus subtilis CsaA with SecA and precursor proteins.";
RL Biochem. J. 348:367-373(2000).
RN [4]
RP PROTEIN SEQUENCE OF 141-182, FUNCTION, IDENTIFICATION OF ACTIVE PEPTIDE,
RP MASS SPECTROMETRY, DISULFIDE BOND, 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 [5]
RP PROTEIN SEQUENCE OF 142-169, FUNCTION IN INDUCTION OF SDPR-SDPI OPERON,
RP SUBCELLULAR LOCATION, 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 SUBUNIT.
RX PubMed=13129613; DOI=10.1016/s0378-1097(03)00578-0;
RA Linde D., Volkmer-Engert R., Schreiber S., Mueller J.P.;
RT "Interaction of the Bacillus subtilis chaperone CsaA with the secretory
RT protein YvaY.";
RL FEMS Microbiol. Lett. 226:93-100(2003).
RN [7]
RP SUBCELLULAR LOCATION, SIGNAL PEPTIDE PROCESSING, AND INDUCTION.
RC STRAIN=168 / DB104;
RX PubMed=14568161; DOI=10.1016/s0378-1097(03)00663-3;
RA Linde D., Marischen L., Mueller J.P.;
RT "Characterisation of preYvaY export reveals differences in the substrate
RT specificities of Bacillus subtilis and Escherichia coli leader
RT peptidases.";
RL FEMS Microbiol. Lett. 227:149-156(2003).
RN [8]
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 [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 FUNCTION.
RC STRAIN=168 / PY79;
RX PubMed=22469514; DOI=10.1111/j.1365-2958.2012.08038.x;
RA Lamsa A., Liu W.T., Dorrestein P.C., Pogliano K.;
RT "The Bacillus subtilis cannibalism toxin SDP collapses the proton motive
RT force and induces autolysis.";
RL Mol. Microbiol. 84:486-500(2012).
RN [11]
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, DISULFIDE BOND, AND MUTAGENESIS
RP OF THR-30; 141-CYS--CYS-147; CYS-141 AND CYS-147.
RC STRAIN=168 / PY79;
RX PubMed=23687264; DOI=10.1128/jb.00407-13;
RA Perez Morales T.G., Ho T.D., Liu W.T., Dorrestein P.C., Ellermeier C.D.;
RT "Production of the cannibalism toxin SDP is a multistep process that
RT requires SdpA and SdpB.";
RL J. Bacteriol. 195:3244-3251(2013).
CC -!- FUNCTION: Produces a 42-residue extracellular sporulation delaying
CC protein (SDP) that collapses the proton motive force (probably both the
CC membrane potential and pH gradient) across the cell membrane, which
CC leads to autolysis; may form a proton channel (PubMed:22469514).
CC Induces the lysis of other B.subtilis cells that have not entered the
CC sporulation pathway, inducing cannibalism to provide a source of
CC nutrients to support sporulation, and at the same time delaying
CC commitment to the energetically expensive and irreversible onset of
CC sporulation (PubMed:12817086). Addition of SDP to liquid cultures halts
CC growth, leads to increased cell permeability and eventually cell lysis
CC in a significant subset of the population, although some cells survive
CC and resume growth after a lag period (PubMed:20805502). Effects of SDP
CC are irreversible within 10 minutes (PubMed:22469514). Addition of SDP
CC to solid cultures induces killing, it is much more effective than SKF
CC (AC O31422) (PubMed:20805502). Has antibiotic action against Gram-
CC positive Firmicutes (L.acidophilus, M.megaterium, P.polymyxa, S.aureus,
CC S.epidermidis) but not Actinobacteria M.luteus or Gram-negative
CC P.aeruginosa or K.pneumoniae (PubMed:20805502, PubMed:22469514). SDP
CC induces expression of the sdpR-sdpI operon (PubMed:12817086). Its
CC maturation is dependent on SdpA and SdpB. Also functions as a ligand,
CC binds to SdpI triggering a signal transduction cascade that protects
CC the cell against the toxic effects of its own SDP.
CC {ECO:0000269|PubMed:12817086, ECO:0000269|PubMed:16469701,
CC ECO:0000269|PubMed:20805502, ECO:0000269|PubMed:22469514}.
CC -!- SUBUNIT: Proprotein probably interacts with chaperone CsaA.
CC {ECO:0000269|PubMed:13129613, ECO:0000305|PubMed:10816431}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12817086,
CC ECO:0000269|PubMed:14568161, ECO:0000269|PubMed:23687264}.
CC Note=Produces a secreted protein originating from this gene
CC (PubMed:12817086), secreted by the general secretory pathway
CC (PubMed:14568161).
CC -!- INDUCTION: By Spo0A during nutrient starvation, through its direct
CC negative control of AbrB (PubMed:12817086). Repressed by AbrB during
CC regular growth when nutrients are plentiful, in association with the
CC transcriptional repressor Abh (PubMed:17720793). Protein not detected
CC during exponential growth, accumulates during stationary phase (at
CC protein level) (PubMed:14568161). {ECO:0000269|PubMed:12817086,
CC ECO:0000269|PubMed:14568161, ECO:0000269|PubMed:17720793}.
CC -!- PTM: Production of active SDP (able to induce SdpI and kill cells) is a
CC multi-step process that requires signal peptide cleavage (probably by
CC SipS or SipT) (PubMed:14568161) as well as SdpA and SdpB. The disulfide
CC bond is not required for maximum toxicity (PubMed:23687264).
CC {ECO:0000269|PubMed:14568161, ECO:0000269|PubMed:23687264}.
CC -!- MASS SPECTROMETRY: [Sporulation delaying protein]: Mass=4311.209;
CC Method=MALDI; Note=Includes a disulfide bond.;
CC Evidence={ECO:0000269|PubMed:20805502};
CC -!- DISRUPTION PHENOTYPE: When the sdpA-sdpB-sdpC operon is deleted,
CC increased rate of spore formation; a double operon deletion (sdpA-sdpC
CC plus skfA-skfH) makes spores even faster (PubMed:12817086). In a single
CC gene deletion no SDP is produced (PubMed:20805502, PubMed:23687264).
CC {ECO:0000269|PubMed:12817086, ECO:0000269|PubMed:20805502,
CC ECO:0000269|PubMed:23687264}.
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";
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DR EMBL; AB006738; BAA21902.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15382.1; -; Genomic_DNA.
DR PIR; B70029; B70029.
DR RefSeq; NP_391257.1; NC_000964.3.
DR RefSeq; WP_003243360.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O34344; -.
DR SMR; O34344; -.
DR STRING; 224308.BSU33770; -.
DR TCDB; 9.B.139.1.1; the pmf-dissipating cannabalism toxin sdpc (sdpc) family.
DR PaxDb; O34344; -.
DR EnsemblBacteria; CAB15382; CAB15382; BSU_33770.
DR GeneID; 936227; -.
DR KEGG; bsu:BSU33770; -.
DR PATRIC; fig|224308.179.peg.3662; -.
DR OMA; DRINAQH; -.
DR BioCyc; BSUB:BSU33770-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0001906; P:cell killing; IDA:UniProtKB.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR InterPro; IPR023888; Antimicrobial_SdpC.
DR TIGRFAMs; TIGR04032; toxin_SdpC; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Bacteriocin; Direct protein sequencing;
KW Disulfide bond; Reference proteome; Secreted; Signal; Toxin; Virulence.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|PubMed:10816431"
FT CHAIN 33..203
FT /note="Sporulation delaying protein C"
FT /evidence="ECO:0000269|PubMed:10816431"
FT /id="PRO_0000435137"
FT PROPEP 33..140
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:20805502"
FT /id="PRO_0000435138"
FT CHAIN 141..182
FT /note="Sporulation delaying protein"
FT /evidence="ECO:0000269|PubMed:20805502"
FT /id="PRO_0000013732"
FT PROPEP 183..203
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:20805502"
FT /id="PRO_0000435139"
FT DISULFID 141..147
FT /evidence="ECO:0000269|PubMed:20805502,
FT ECO:0000269|PubMed:23687264"
FT MUTAGEN 30
FT /note="T->H: Reduced amounts of pro-SdpC produced, no
FT proSdpC is secreted, decreased amounts of SdpI expressed,
FT decreased toxicity."
FT /evidence="ECO:0000269|PubMed:23687264"
FT MUTAGEN 141..147
FT /note="CGLYAVC->AGLYAVA: 7-fold decrease in induction of
FT SdpI, decreased toxicity of SDP."
FT /evidence="ECO:0000269|PubMed:23687264"
FT MUTAGEN 141
FT /note="C->A: 7-fold decrease in induction of SdpI,
FT decreased toxicity of SDP."
FT /evidence="ECO:0000269|PubMed:23687264"
FT MUTAGEN 147
FT /note="C->A: 7-fold decrease in induction of SdpI,
FT decreased toxicity of SDP."
FT /evidence="ECO:0000269|PubMed:23687264"
FT CONFLICT 161
FT /note="Missing (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
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
