P29142 (SUBT_GEOSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 72.
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: Subtilisin J EC=3.4.21.62 | ||
| Gene names |
| ||
| Organism | Geobacillus stearothermophilus (Bacillus stearothermophilus) | ||
| Taxonomic identifier | 1422 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus |
Protein attributes
| Sequence length | 381 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. |
| Catalytic activity | Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides. |
| Cofactor | Binds 2 calcium ions per subunit By similarity. |
| Subcellular location | |
| Miscellaneous | Secretion of subtilisin is associated with onset of sporulation, and many mutations which block sporulation at early stages affect expression levels of subtilisin. However, subtilisin is not necessary for normal sporulation. |
| Sequence similarities | Belongs to the peptidase S8 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Sporulation |
| Cellular component | Secreted |
| Domain | Signal |
| Ligand | Calcium Metal-binding |
| Molecular function | Hydrolase Protease Serine protease |
| PTM | Zymogen |
| Gene Ontology (GO) | |
| Biological process | negative regulation of catalytic activity Inferred from electronic annotation. Source: InterPro proteolysisInferred from electronic annotation. Source: UniProtKB-KW sporulation resulting in formation of a cellular sporeInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | identical protein binding Inferred from electronic annotation. Source: InterPro metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 29 | 29 | Potential | ||||||
| Propeptide | 30 – 106 | 77 | Potential | PRO_0000027185 | |||||
| Chain | 107 – 381 | 275 | Subtilisin J | PRO_0000027186 | |||||
Sites | |||||||||
| Active site | 138 | 1 | Charge relay system By similarity | ||||||
| Active site | 170 | 1 | Charge relay system By similarity | ||||||
| Active site | 327 | 1 | Charge relay system By similarity | ||||||
| Metal binding | 108 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 147 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 181 | 1 | Calcium 1; via carbonyl oxygen By similarity | ||||||
| Metal binding | 183 | 1 | Calcium 1 By similarity | ||||||
| Metal binding | 185 | 1 | Calcium 1; via carbonyl oxygen By similarity | ||||||
| Metal binding | 187 | 1 | Calcium 1; via carbonyl oxygen By similarity | ||||||
| Metal binding | 275 | 1 | Calcium 2; via carbonyl oxygen By similarity | ||||||
| Metal binding | 277 | 1 | Calcium 2; via carbonyl oxygen By similarity | ||||||
| Metal binding | 280 | 1 | Calcium 2; via carbonyl oxygen By similarity | ||||||
Sequences
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References
| [1] | "Molecular cloning of a subtilisin J gene from Bacillus stearothermophilus and its expression in Bacillus subtilis." Jang J.S., Kang D.O., Chun M.J., Byun S.M. Biochem. Biophys. Res. Commun. 184:277-282(1992) [PubMed: 1567435] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DSM 2313 / NCIMB 10278 / KCTC 1823. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M64743 Genomic DNA. Translation: AAA22247.1. |
| PIR | JQ1487. |
3D structure databases | |
| ProteinModelPortal | P29142. |
| SMR | P29142. Positions 36-381. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S08.035. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR000209. Peptidase_S8/S53. IPR023827. Peptidase_S8_Asp-AS. IPR022398. Peptidase_S8_His-AS. IPR023828. Peptidase_S8_Ser-AS. IPR015500. Peptidase_S8_subtilisin-rel. IPR009020. Prot_inh_propept. IPR010259. Prot_inh_S8A. [Graphical view] |
| Gene3D | G3DSA:3.40.50.200. Pept_S8_S53. 1 hit. |
| PANTHER | PTHR10795. SubtilSerProt. 1 hit. |
| Pfam | PF05922. Inhibitor_I9. 1 hit. PF00082. Peptidase_S8. 1 hit. [Graphical view] |
| PRINTS | PR00723. SUBTILISIN. |
| SUPFAM | SSF52743. Pept_S8_S53. 1 hit. SSF54897. Prot_inh_propept. 1 hit. |
| PROSITE | PS00136. SUBTILASE_ASP. 1 hit. PS00137. SUBTILASE_HIS. 1 hit. PS00138. SUBTILASE_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SUBT_GEOSE | ||||||||
| Accession | Primary (citable) accession number: P29142 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with