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Protein

Sporulation killing factor

Gene

skfA

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

Functioni

Produces a 26-residue extracellular sporulation filling factor (SKF) that induces the lysis of other B.subtilis cells that have not entered the sporulation pathway, providing 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, PubMed:20805502). Can also inhibit growth of other bacteria at high concentrations (PubMed:11851812). Addition of SKF to solid cultures induces killing, but it is much less effective than SDP (AC O34344) (PubMed:20805502). Has a role in protecting the secreted lipase LipA against proteolysis, either by modulating its folding or by acting as a protease inhibitor (PubMed:15812018).4 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Bacteriocin

Enzyme and pathway databases

BioCyciBSUB:BSU01910-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Sporulation killing factor1 Publication
Short name:
SKF1 Publication
Alternative name(s):
Sporulation-killing factor SkfA
Gene namesi
Name:skfA1 Publication
Synonyms:ybcO
Ordered Locus Names:BSU01910
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

When the skfA-skfB-skfC-skfE-skfF-skfG-skfH 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 SKP is produced (PubMed:20805502).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 2929Missing : Cys-Met cross-link not made. 1 PublicationAdd
BLAST
Mutagenesisi33 – 419CWASKSIAM → MWASKSIAC: Cys-Met cross-link not made, suggests relative amino acid positions are important for thioether bond formation. 1 Publication
Mutagenesisi33 – 331C → A or S: Cys-thioether cross-link not made. 1 Publication
Mutagenesisi41 – 411M → A, F, L or Y: Approximately wild-type amounts of Cys-thioether cross-link made. 1 Publication
Mutagenesisi41 – 411M → E, K or Q: Cys-thioether cross-link not made. 1 Publication
Mutagenesisi41 – 411M → N, S or T: 50% wild-type amount of Cys-thioether cross-link made. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 29291 PublicationPRO_0000435140Add
BLAST
Peptidei30 – 5526Sporulation killing factor1 PublicationPRO_0000049459Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki30 ↔ 55Cyclopeptide (Cys-Ile)1 Publication
Disulfide bondi30 ↔ 451 Publication
Cross-linki33 ↔ 412-(S-cysteinyl)-methionine (Cys-Met)2 Publications

Post-translational modificationi

This is a cyclic peptide (PubMed:20805502, PubMed:23282011). The first step in SKF maturation is probably thioether bond formation (PubMed:23282011).2 Publications

Keywords - PTMi

Disulfide bond, Thioether bond

Proteomic databases

PaxDbiO31422.

Expressioni

Inductioni

By Spo0A (PubMed:12817086) and PhoP (PubMed:16816204), during nutrient starvation, especially phosphate starvation. Repressed by AbrB during normal growth when nutrients are plentiful, in association with the transcriptional repressor Abh.4 Publications

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100001078.

Family & Domainsi

Family and domain databases

InterProiIPR030919. RiPP_SkfA.
[Graphical view]
TIGRFAMsiTIGR04404. RiPP_SkfA. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O31422-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRNQKEWES VSKKGLMKPG GTSIVKAAGC MGCWASKSIA MTRVCALPHP

AMRAI
Length:55
Mass (Da):5,934
Last modified:January 1, 1998 - v1
Checksum:iF169E627ADBEBB55
GO

Mass spectrometryi

Molecular mass is 2781.302 Da from positions 30 - 55. Determined by MALDI. Cyclic, disulfide-containing sactipeptide with a thioether cross-link of cysteine to methionine.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB006424 Genomic DNA. Translation: BAA33086.1.
AL009126 Genomic DNA. Translation: CAB11984.1.
PIRiC69746.
RefSeqiNP_388072.1. NC_000964.3.
WP_009966416.1. NZ_JNCM01000030.1.

Genome annotation databases

EnsemblBacteriaiCAB11984; CAB11984; BSU01910.
GeneIDi938506.
KEGGibsu:BSU01910.
PATRICi38335271. VBIBacSub146942_0192.

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
AB006424 Genomic DNA. Translation: BAA33086.1.
AL009126 Genomic DNA. Translation: CAB11984.1.
PIRiC69746.
RefSeqiNP_388072.1. NC_000964.3.
WP_009966416.1. NZ_JNCM01000030.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100001078.

Proteomic databases

PaxDbiO31422.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB11984; CAB11984; BSU01910.
GeneIDi938506.
KEGGibsu:BSU01910.
PATRICi38335271. VBIBacSub146942_0192.

Enzyme and pathway databases

BioCyciBSUB:BSU01910-MONOMER.

Family and domain databases

InterProiIPR030919. RiPP_SkfA.
[Graphical view]
TIGRFAMsiTIGR04404. RiPP_SkfA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSKFA_BACSU
AccessioniPrimary (citable) accession number: O31422
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: January 1, 1998
Last modified: March 16, 2016
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Accelerated cannibalism by skf- cells is seen on solid media but not in liquid media.1 Publication

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

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.