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Protein

Sporulation delaying protein C

Gene

sdpC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Produces a 42-residue extracellular sporulation delaying protein (SDP) that collapses the proton motive force (probably both the membrane potential and pH gradient) across the cell membrane, which leads to autolysis; may form a proton channel (PubMed:22469514). Induces the lysis of other B.subtilis cells that have not entered the sporulation pathway, inducing cannibalism to provide a source of nutrients to support sporulation, and at the same time delaying commitment to the energetically expensive and irreversible onset of sporulation (PubMed:12817086). Addition of SDP to liquid cultures halts growth, leads to increased cell permeability and eventually cell lysis in a significant subset of the population, although some cells survive and resume growth after a lag period (PubMed:20805502). Effects of SDP are irreversible within 10 minutes (PubMed:22469514). Addition of SDP to solid cultures induces killing, it is much more effective than SKF (AC O31422) (PubMed:20805502). Has antibiotic action against Gram-positive Firmicutes (L.acidophilus, M.megaterium, P.polymyxa, S.aureus, S.epidermidis) but not Actinobacteria M.luteus or Gram-negative P.aeruginosa or K.pneumoniae (PubMed:20805502, PubMed:22469514). SDP induces expression of the sdpR-sdpI operon (PubMed:12817086). Its maturation is dependent on SdpA and SdpB. Also functions as a ligand, binds to SdpI triggering a signal transduction cascade that protects the cell against the toxic effects of its own SDP.4 Publications

GO - Biological processi

  • cell killing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Bacteriocin, Toxin

Enzyme and pathway databases

BioCyciBSUB:BSU33770-MONOMER.

Protein family/group databases

TCDBi9.B.139.1.1. the cannabalism toxin sdpc (sdpc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Sporulation delaying protein C1 Publication
Short name:
SdpC
Alternative name(s):
Cannibalism toxin SDP1 Publication
Killing factor SdpC
Toxic peptide SdpC
Cleaved into the following chain:
Sporulation delaying protein1 Publication
Short name:
SDP1 Publication
Gene namesi
Name:sdpC1 Publication
Synonyms:yvaY
Ordered Locus Names:BSU33770
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU33770. [Micado]

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

When the sdpA-sdpB-sdpC operon is deleted, increased rate of spore formation; a double operon deletion (sdpA-sdpC plus skfA-skfH) makes spores even faster (PubMed:12817086). In a single gene deletion no SDP is produced (PubMed:20805502, PubMed:23687264).3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi30 – 301T → H: Reduced amounts of pro-SdpC produced, no proSdpC is secreted, decreased amounts of SdpI expressed, decreased toxicity. 1 Publication
Mutagenesisi141 – 1477CGLYAVC → AGLYAVA: 7-fold decrease in induction of SdpI, decreased toxicity of SDP. 1 Publication
Mutagenesisi141 – 1411C → A: 7-fold decrease in induction of SdpI, decreased toxicity of SDP. 1 Publication
Mutagenesisi147 – 1471C → A: 7-fold decrease in induction of SdpI, decreased toxicity of SDP. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 32321 PublicationAdd
BLAST
Chaini33 – 203171Sporulation delaying protein C1 PublicationPRO_0000435137Add
BLAST
Propeptidei33 – 140108Removed in mature form1 PublicationPRO_0000435138Add
BLAST
Chaini141 – 18242Sporulation delaying protein1 PublicationPRO_0000013732Add
BLAST
Propeptidei183 – 20321Removed in mature form1 PublicationPRO_0000435139Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi141 ↔ 1472 Publications

Post-translational modificationi

Production of active SDP (able to induce SdpI and kill cells) is a multi-step process that requires signal peptide cleavage (probably by SipS or SipT) (PubMed:14568161) as well as SdpA and SdpB. The disulfide bond is not required for maximum toxicity (PubMed:23687264).2 Publications

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiO34344.

Expressioni

Inductioni

By Spo0A during nutrient starvation, through its direct negative control of AbrB (PubMed:12817086). Repressed by AbrB during regular growth when nutrients are plentiful, in association with the transcriptional repressor Abh (PubMed:17720793). Protein not detected during exponential growth, accumulates during stationary phase (at protein level) (PubMed:14568161).3 Publications

Interactioni

Subunit structurei

Proprotein probably interacts with chaperone CsaA.1 Publication1 Publication

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100018321.

Family & Domainsi

Keywords - Domaini

Signal

Phylogenomic databases

OMAiDRINAQH.
OrthoDBiEOG618R3B.

Family and domain databases

InterProiIPR023888. Antimicrobial_SdpC.
[Graphical view]
TIGRFAMsiTIGR04032. toxin_SdpC. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O34344-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSKLLRLLI VSMVTILVFS LVGLSKESST SAKENHTFSG EDYFRGLLFG
60 70 80 90 100
QGEVGKLISN DLDPKLVKEA NSTEGKKLVN DVVKFIKKDQ PQYMDELKQS
110 120 130 140 150
IDSKDPKKLI ENMTKADQLI QKYAKKNENV KYSSNKVTPS CGLYAVCVAA
160 170 180 190 200
GYLYVVGVNA VALQTAAAVT TAVWKYVAKY SSSASNNSDL EAAAAKTLKL

IHQ
Length:203
Mass (Da):22,221
Last modified:January 1, 1998 - v1
Checksum:i4928C22C6AB4BEBC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti161 – 1611Missing AA sequence (PubMed:12817086).Curated

Mass spectrometryi

Molecular mass is 4311.209 Da from positions 141 - 182. Determined by MALDI. Includes a disulfide bond.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006738 Genomic DNA. Translation: BAA21902.1.
AL009126 Genomic DNA. Translation: CAB15382.1.
PIRiB70029.
RefSeqiNP_391257.1. NC_000964.3.
WP_003243360.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15382; CAB15382; BSU33770.
GeneIDi936227.
KEGGibsu:BSU33770.
PATRICi18978754. VBIBacSub10457_3540.

Cross-referencesi

Web resourcesi

Protein Spotlight

I'll have you for supper - Issue 90 of January 2008

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006738 Genomic DNA. Translation: BAA21902.1.
AL009126 Genomic DNA. Translation: CAB15382.1.
PIRiB70029.
RefSeqiNP_391257.1. NC_000964.3.
WP_003243360.1. NZ_JNCM01000033.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100018321.

Protein family/group databases

TCDBi9.B.139.1.1. the cannabalism toxin sdpc (sdpc) family.

Proteomic databases

PaxDbiO34344.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15382; CAB15382; BSU33770.
GeneIDi936227.
KEGGibsu:BSU33770.
PATRICi18978754. VBIBacSub10457_3540.

Organism-specific databases

GenoListiBSU33770. [Micado]

Phylogenomic databases

OMAiDRINAQH.
OrthoDBiEOG618R3B.

Enzyme and pathway databases

BioCyciBSUB:BSU33770-MONOMER.

Family and domain databases

InterProiIPR023888. Antimicrobial_SdpC.
[Graphical view]
TIGRFAMsiTIGR04032. toxin_SdpC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Nakamura A., Grau R., Perego M., Hoch J.A.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / JH642.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Interaction of Bacillus subtilis CsaA with SecA and precursor proteins."
    Mueller J.P., Ozegowski J., Vettermann S., Swaving J., Van Wely K.H., Driessen A.J.
    Biochem. J. 348:367-373(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 33-42, SUBUNIT.
    Strain: 168 / DB104.
  4. "Imaging mass spectrometry of intraspecies metabolic exchange revealed the cannibalistic factors of Bacillus subtilis."
    Liu W.T., Yang Y.L., Xu Y., Lamsa A., Haste N.M., Yang J.Y., Ng J., Gonzalez D., Ellermeier C.D., Straight P.D., Pevzner P.A., Pogliano J., Nizet V., Pogliano K., Dorrestein P.C.
    Proc. Natl. Acad. Sci. U.S.A. 107:16286-16290(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 141-182, FUNCTION, IDENTIFICATION OF ACTIVE PEPTIDE, MASS SPECTROMETRY, DISULFIDE BOND, DISRUPTION PHENOTYPE.
    Strain: 168 / PY79.
  5. Cited for: PROTEIN SEQUENCE OF 142-169, FUNCTION IN INDUCTION OF SDPR-SDPI OPERON, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE.
    Strain: 168 / PY79.
  6. "Interaction of the Bacillus subtilis chaperone CsaA with the secretory protein YvaY."
    Linde D., Volkmer-Engert R., Schreiber S., Mueller J.P.
    FEMS Microbiol. Lett. 226:93-100(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  7. "Characterisation of preYvaY export reveals differences in the substrate specificities of Bacillus subtilis and Escherichia coli leader peptidases."
    Linde D., Marischen L., Mueller J.P.
    FEMS Microbiol. Lett. 227:149-156(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SIGNAL PEPTIDE PROCESSING, INDUCTION.
    Strain: 168 / DB104.
  8. "A three-protein signaling pathway governing immunity to a bacterial cannibalism toxin."
    Ellermeier C.D., Hobbs E.C., Gonzalez-Pastor J.E., Losick R.
    Cell 124:549-559(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: 168 / PY79.
  9. "Abh and AbrB control of Bacillus subtilis antimicrobial gene expression."
    Strauch M.A., Bobay B.G., Cavanagh J., Yao F., Wilson A., Le Breton Y.
    J. Bacteriol. 189:7720-7732(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: REPRESSION BY ABRB AND ABH.
  10. "The Bacillus subtilis cannibalism toxin SDP collapses the proton motive force and induces autolysis."
    Lamsa A., Liu W.T., Dorrestein P.C., Pogliano K.
    Mol. Microbiol. 84:486-500(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: 168 / PY79.
  11. "Production of the cannibalism toxin SDP is a multistep process that requires SdpA and SdpB."
    Perez Morales T.G., Ho T.D., Liu W.T., Dorrestein P.C., Ellermeier C.D.
    J. Bacteriol. 195:3244-3251(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, DISULFIDE BOND, MUTAGENESIS OF THR-30; 141-CYS--CYS-147; CYS-141 AND CYS-147.
    Strain: 168 / PY79.

Entry informationi

Entry nameiSDPC_BACSU
AccessioniPrimary (citable) accession number: O34344
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: January 1, 1998
Last modified: January 20, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.