O07623 (SBOA_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 83.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Subtilosin-A Alternative name(s): Antilisterial bacteriocin subtilosin | ||||||
| Gene names |
| ||||||
| Organism | Bacillus subtilis (strain 168) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 224308 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › ![]() |
Protein attributes
| Sequence length | 43 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Has bacteriocidal activity against some Gram-positive bacteria such as Listeria, some species of Bacillus and E.faecium. Ref.5 |
| Subcellular location | |
| Developmental stage | The production of subtilosin A begins at the end of vegetative growth and finishes before spore formation. |
| Induction | Transcription is highly induced by oxygen limitation and is under dual and independent control of Spo0A-AbrB and ResDE. Ref.6 |
| Post-translational modification | This peptide 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. 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. In forming these cross-links, Thr-36 and Phe-39 are converted to D-amino-acids. |
| Sequence similarities | Belongs to the bacteriocin class V family. |
| Caution | Ref.4 sequence does not report residues in positions 30 and 39 probably due to their modification, and reports a cyclic permutation of the peptide sequence. |
| Mass spectrometry | Molecular mass is 3398.9 Da from positions 9 - 43. Determined by FAB. Ref.4 |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Molecular function | Antibiotic Antimicrobial Bacteriocin |
| PTM | D-amino acid Thioether bond |
| Technical term | 3D-structure Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacteriumInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||
Molecule processing | |||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Propeptide | 1 – 8 | 8 | PRO_0000002780 | ||||||||||||
| Peptide | 9 – 43 | 35 | Subtilosin-A Ref.4 | PRO_0000002781 | |||||||||||
Amino acid modifications | |||||||||||||||
| Cross-link | 9 ↔ 43 | Cyclopeptide (Asn-Gly) | |||||||||||||
| Cross-link | 12 ↔ 39 | 2-cysteinyl-D-phenylalanine (Cys-Phe) | |||||||||||||
| Cross-link | 15 ↔ 36 | 2-cysteinyl-D-allo-threonine (Cys-Thr) | |||||||||||||
| Cross-link | 21 ↔ 30 | 2-cysteinyl-L-phenylalanine (Cys-Phe) | |||||||||||||
Secondary structure | |||||||||||||||
Helix Strand Turn | |||||||||||||||
| Turn | 12 – 15 | 4 | |||||||||||||
| Turn | 23 – 26 | 4 | |||||||||||||
| Helix | 37 – 42 | 6 | |||||||||||||
Sequences
References
| « Hide 'large scale' references | |
| [1] | "Subtilosin A biosynthesis is conserved among two different classes of Bacillus subtilis strains." Stein T., Duesterhus S., Entian K.-D. Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 6633 / PCI 219 / NRS 231. |
| [2] | "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees)." Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P. Microbiology 143:3313-3328(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [3] | "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. Danchin A.Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [4] | "Subtilosin A, a new antibiotic peptide produced by Bacillus subtilis 168: isolation, structural analysis, and biogenesis." Babasaki K., Takao T., Shimonishi Y., Kurahashi K. J. Biochem. 98:585-603(1985) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 9-43, CHARACTERIZATION, MASS SPECTROMETRY. Strain: 168. |
| [5] | "Genes of the sbo-alb locus of Bacillus subtilis are required for production of the antilisterial bacteriocin subtilosin." Zheng G., Yan L.Z., Vederas J.C., Zuber P. J. Bacteriol. 181:7346-7355(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. Strain: 168 / JH642 and 22a. |
| [6] | "Dual control of sbo-alb operon expression by the Spo0 and ResDE systems of signal transduction under anaerobic conditions in Bacillus subtilis." Nakano M.M., Zheng G., Zuber P. J. Bacteriol. 182:3274-3277(2000) [PubMed] [Europe PMC] [Abstract] Cited for: TRANSCRIPTIONAL REGULATION. Strain: 168 / JH642. |
| [7] | "Structure of subtilosin A, an antimicrobial peptide from Bacillus subtilis with unusual posttranslational modifications linking cysteine sulfurs to alpha-carbons of phenylalanine and threonine." Kawulka K., Sprules T., McKay R.T., Mercier P., Diaper C.M., Zuber P., Vederas J.C. J. Am. Chem. Soc. 125:4726-4727(2003) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR, CROSS-LINKS CYS-PHE AND CYS-THR. |
| [8] | Vederas J.C. Unpublished observations (MAY-2003) Cited for: STEREOCHEMISTRY OF D-ALLO-THR-36. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AJ430547 Genomic DNA. Translation: CAD23198.1. Z97024 Genomic DNA. Translation: CAB09701.1. AL009126 Genomic DNA. Translation: CAB15763.1. | ||||||||||||
| PIR | A69704. | ||||||||||||
| RefSeq | NP_391616.1. NC_000964.3. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | O07623. | ||||||||||||
| SMR | O07623. Positions 9-43. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| STRING | 224308.BSU37350. | ||||||||||||
Protein family/group databases | |||||||||||||
| TCDB | 1.C.84.1.1. subtilosin family. | ||||||||||||
Proteomic databases | |||||||||||||
| PaxDb | O07623. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | CAB15763; CAB15763; BSU37350. | ||||||||||||
| GeneID | 938512. | ||||||||||||
| KEGG | bsu:BSU37350. | ||||||||||||
| PATRIC | 18979508. VBIBacSub10457_3916. | ||||||||||||
Organism-specific databases | |||||||||||||
| GenoList | BSU37350. [Micado] | ||||||||||||
Phylogenomic databases | |||||||||||||
| ProtClustDB | CLSK2752544. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | BSUB:BSU37350-MONOMER. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR021539. Subtilosin_A. [Graphical view] | ||||||||||||
| Pfam | PF11420. Subtilosin_A. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | O07623. | ||||||||||||
Entry information
| Entry name | SBOA_BACSU | ||||||||
| Accession | Primary (citable) accession number: O07623 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
