Reviewed,
UniProtKB/Swiss-Prot Q8G4D1 (GCP_BIFLO)
Last modified
February 9, 2010.
Version 39.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Probable O-sialoglycoprotein endopeptidase Short name=Glycoprotease EC=3.4.24.57 | ||||
| Gene names |
| ||||
| Organism | Bifidobacterium longum [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 216816 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium |
Protein attributes
| Sequence length | 347 AA. |
| Sequence status | Complete. |
| 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 Probable. HAMAP MF_01445 |
| 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 – 347 | 347 | Probable O-sialoglycoprotein endopeptidase HAMAP MF_01445 | PRO_0000303281 | |||||
Sites | |||||||||
| Metal binding | 113 | 1 | Zinc Potential | ||||||
| Metal binding | 117 | 1 | Zinc Potential | ||||||
Sequences
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References
| [1] | "The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract." Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F. Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed: 12381787] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCC 2705. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014295 Genomic DNA. Translation: AAN25252.1. |
| RefSeq | NP_696616.1. |
3D structure databases | |
| SMR | Q8G4D1. Positions 5-331. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | M22.001. |
Genome annotation databases | |
| GeneID | 1021610. |
| GenomeReviews | Gene locus BL1457 in contig AE014295_GR. |
| KEGG | blo:BL1457. |
| NMPDR | fig|206672.1.peg.1383. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG304663. |
| OMA | EHSAYGG. |
| PhylomeDB | Q8G4D1. |
Enzyme and pathway databases | |
| BioCyc | BLON206672:BL1457-MONOMER. |
| BRENDA | 3.4.24.57. 39917. |
Family and domain databases | |
| HAMAP | MF_01445. Glycoptase_bact. [Tree] |
| InterPro | IPR009180. Pept_M22_O-sialoglycoprot. IPR000905. Peptidase_M22. 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. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GCP_BIFLO | ||||||||
| Accession | Primary (citable) accession number: Q8G4D1 | ||||||||
| 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 |

Clusters with


