Reviewed,
UniProtKB/Swiss-Prot B5RMW0 (GCP_BORDL)
Last modified
November 3, 2009.
Version 9.
History...
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90%,
50% identity |
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Probable O-sialoglycoprotein endopeptidase Short name=Glycoprotease EC=3.4.24.57 | ||||
| Gene names |
| ||||
| Organism | Borrelia duttonii (strain Ly) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 412419 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia |
Protein attributes
| Sequence length | 338 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | Hydrolysis of O-sialoglycoproteins; cleaves 31-Arg-|-Asp-32 bond in glycophorin A. Does not cleave unglycosylated proteins, desialylated glycoproteins or glycoproteins that are only N-glycosylated. HAMAP MF_01445 |
| Cofactor | Zinc By similarity. |
| Sequence similarities | Belongs to the peptidase M22 family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Metal-binding Zinc |
| Molecular function | Hydrolase Metalloprotease Protease |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: InterPro |
| Molecular function | metalloendopeptidase activity Inferred from electronic annotation. Source: HAMAP zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 338 | 338 | Probable O-sialoglycoprotein endopeptidase HAMAP MF_01445 | PRO_1000145949 | |||||
Sites | |||||||||
| Metal binding | 110 | 1 | Zinc Potential | ||||||
| Metal binding | 114 | 1 | Zinc Potential | ||||||
Sequences
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References
| [1] | "The genome of Borrelia recurrentis, the agent of deadly louse-borne relapsing fever, is a degraded subset of tick-borne Borrelia duttonii." Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J., Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M. PLoS Genet. 4:E1000185-E1000185(2008) [PubMed: 18787695] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000976 Genomic DNA. Translation: ACH93696.1. | |
| RefSeq | YP_002222402.1. |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | M22.001. |
Genome annotation databases | |
| GeneID | 6917999. |
| GenomeReviews | Gene locus BDU_773 in contig CP000976_GR. |
| KEGG | bdu:BDU_773. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | CKRALKQ. |
Family and domain databases | |
| HAMAP | MF_01445. [Tree] |
| InterPro | IPR009180. Pept_M22_Osialgl. IPR000905. Peptidase_M22. IPR017860. Peptidase_M22_CS. IPR017861. Peptidase_M22_subgr. [Graphical view] |
| PANTHER | PTHR11735. Pept_M22_Osialgl. 1 hit. |
| Pfam | PF00814. Peptidase_M22. 1 hit. [Graphical view] |
| PRINTS | PR00789. OSIALOPTASE. |
| TIGRFAMs | TIGR00329. gcp. 1 hit. |
| PROSITE | PS01016. GLYCOPROTEASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GCP_BORDL | ||||||||
| Accession | Primary (citable) accession number: B5RMW0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

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