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Protein

Subtilosin-A

Gene

sboA

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

Functioni

Has bacteriocidal activity against some Gram-positive bacteria such as Listeria, some species of Bacillus and E.faecium (PubMed:10572140, PubMed:19633086, PubMed:3936839). A single mutation (Thr-14-Ile) confers hemolytic activity against rabbit and human blood (PubMed:19633086).3 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Bacteriocin

Enzyme and pathway databases

BioCyciBSUB:BSU37350-MONOMER.

Protein family/group databases

TCDBi1.C.84.1.1. the subtilosin (subtilosin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Subtilosin-A
Alternative name(s):
Antilisterial bacteriocin subtilosin
Gene namesi
Name:sboA
Synonyms:sbo
Ordered Locus Names:BSU37350
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1 – 8Missing : No thioether bonds formed. 1 Publication8
Mutagenesisi12C → A in vitro no longer makes the first thioether cross-link, in vivo no cyclopeptide formed. 1 Publication1
Mutagenesisi12C → S in vivo forms 2 thioether cross-links, no cyclopeptide formed. 1 Publication1
Mutagenesisi14T → I in sboA1; protein has acquired hemolytic activity and is more effective against tested Gram-positive bacteria. 1 Publication1
Mutagenesisi15C → A in vitro can no longer make the Cys-thioether cross-link, variable loss of the other 2 thioether cross-links, in vivo no cyclopeptide formed. 1 Publication1
Mutagenesisi15C → S in vivo forms 2 thioether cross-links, no cyclopeptide formed. 1 Publication1
Mutagenesisi21C → A in vitro no longer makes the second thioether cross-link, in vivo no cyclopeptide formed. 1 Publication1
Mutagenesisi21C → S in vivo forms 2 thioether cross-links, no cyclopeptide formed. 1 Publication1
Mutagenesisi30F → S in vivo forms 2 thioether cross-links, no cyclopeptide formed. 1 Publication1
Mutagenesisi36T → S in vivo forms 2 thioether cross-links, no cyclopeptide formed. 1 Publication1
Mutagenesisi39F → S in vivo forms 2 thioether cross-links, no cyclopeptide formed. 1 Publication1
Mutagenesisi39F → Y in vivo forms 3 thioether cross-links, forms the cyclopeptide. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000027801 – 81 Publication8
PeptideiPRO_00000027819 – 43Subtilosin-A1 PublicationAdd BLAST35

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki9 ↔ 43Cyclopeptide (Asn-Gly)1 Publication
Cross-linki12 ↔ 392-cysteinyl-D-phenylalanine (Cys-Phe)2 Publications
Cross-linki15 ↔ 362-cysteinyl-D-allo-threonine (Cys-Thr)2 Publications
Cross-linki21 ↔ 302-cysteinyl-L-phenylalanine (Cys-Phe)2 Publications

Post-translational modificationi

This sactipeptide undergoes unique processing steps that include proteolytic cleavage after Glu-8, and covalent linkage of the alpha-amino of Asn-9 with the carboxyl of Gly-43 to form a cyclopeptide (PubMed:12696888, PubMed:22366720). Thioether cross-links are formed between cysteines and the alpha-carbons of other amino acids, Cys-12 to Phe-39, Cys-15 to Thr-36, and Cys-21 to Phe-30 (PubMed:12696888, PubMed:22366720). In forming these cross-links, Thr-36 and Phe-39 are converted to D-amino acids (PubMed:12696888). Propeptide cleavage and cyclopeptide formation only occur after all 3 thioether cross-links are formed (PubMed:22366720).2 Publications

Keywords - PTMi

D-amino acid, Thioether bond

Proteomic databases

PaxDbiO07623.

Expressioni

Developmental stagei

The production of subtilosin A begins at the end of vegetative growth and finishes before spore formation.1 Publication

Inductioni

Transcription is highly induced by oxygen limitation and is under dual and independent control of Spo0A-AbrB and ResDE.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100020186.

Structurei

Secondary structure

143
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni12 – 15Combined sources4
Turni23 – 26Combined sources4
Helixi37 – 42Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PXQNMR-A9-43[»]
ProteinModelPortaliO07623.
SMRiO07623.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO07623.

Family & Domainsi

Sequence similaritiesi

Belongs to the bacteriocin class V family.Curated

Family and domain databases

InterProiIPR021539. Subtilosin_A.
[Graphical view]
PfamiPF11420. Subtilosin_A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O07623-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40 
MKKAVIVENK GCATCSIGAA CLVDGPIPDF EIAGATGLFG LWG
Length:43
Mass (Da):4,325
Last modified:July 1, 1997 - v1
Checksum:i055A81DA0D378794
GO

Mass spectrometryi

Molecular mass is 3398.9 Da from positions 9 - 43. Determined by FAB. 1 Publication
Molecular mass is 3412.5 Da from positions 9 - 43. Determined by MALDI. The Thr-14-Ile mutant.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ430547 Genomic DNA. Translation: CAD23198.1.
Z97024 Genomic DNA. Translation: CAB09701.1.
AL009126 Genomic DNA. Translation: CAB15763.1.
PIRiA69704.
RefSeqiNP_391616.1. NC_000964.3.
WP_003222002.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB15763; CAB15763; BSU37350.
GeneIDi23411752.
938512.
KEGGibsu:BSU37350.
PATRICi18979508. VBIBacSub10457_3916.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ430547 Genomic DNA. Translation: CAD23198.1.
Z97024 Genomic DNA. Translation: CAB09701.1.
AL009126 Genomic DNA. Translation: CAB15763.1.
PIRiA69704.
RefSeqiNP_391616.1. NC_000964.3.
WP_003222002.1. NZ_JNCM01000034.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PXQNMR-A9-43[»]
ProteinModelPortaliO07623.
SMRiO07623.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100020186.

Protein family/group databases

TCDBi1.C.84.1.1. the subtilosin (subtilosin) family.

Proteomic databases

PaxDbiO07623.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15763; CAB15763; BSU37350.
GeneIDi23411752.
938512.
KEGGibsu:BSU37350.
PATRICi18979508. VBIBacSub10457_3916.

Enzyme and pathway databases

BioCyciBSUB:BSU37350-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO07623.

Family and domain databases

InterProiIPR021539. Subtilosin_A.
[Graphical view]
PfamiPF11420. Subtilosin_A. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSBOA_BACSU
AccessioniPrimary (citable) accession number: O07623
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: July 1, 1997
Last modified: November 2, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

PubMed:3936839 sequence does not report residues in positions 30 and 39 probably due to their modification, and reports a cyclic permutation of the peptide sequence.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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.