B2IQS1 (DEF_STRPS) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 24.
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: Peptide deformylase Short name=PDF EC=3.5.1.88 Alternative name(s): Polypeptide deformylase | ||||
| Gene names |
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| Organism | Streptococcus pneumoniae (strain CGSP14) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 516950 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus |
Protein attributes
| Sequence length | 203 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions By similarity. HAMAP MF_00163 |
| Catalytic activity | Formyl-L-methionyl peptide + H2O = formate + methionyl peptide. HAMAP MF_00163 |
| Cofactor | Binds 1 Fe2+ ion By similarity. HAMAP MF_00163 |
| Sequence similarities | Belongs to the polypeptide deformylase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Ligand | Iron Metal-binding |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | translation Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | iron ion binding Inferred from electronic annotation. Source: InterPro peptide deformylase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Genome evolution driven by host adaptations results in a more virulent and antimicrobial-resistant Streptococcus pneumoniae serotype 14." Ding F., Tang P., Hsu M.-H., Cui P., Hu S., Yu J., Chiu C.-H. BMC Genomics 10:158-158(2009) [PubMed: 19361343] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CGSP14. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001033 Genomic DNA. Translation: ACB90695.1. |
| RefSeq | YP_001836160.1. NC_010582.1. |
3D structure databases | |
| ProteinModelPortal | B2IQS1. |
| SMR | B2IQS1. Positions 2-203. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B2IQS1. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBSTRT00000018150; EBSTRP00000017464; EBSTRG00000018150. |
| GeneID | 6217864. |
| GenomeReviews | Gene locus SPCG_1443 in contig CP001033_GR. |
| KEGG | spw:SPCG_1443. |
| PATRIC | 19679172. VBIStrPne123335_1542. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000026595. |
| HOGENOM | HBG665227. |
| OMA | ADGEGCL. |
| ProtClustDB | PRK00150. |
Family and domain databases | |
| HAMAP | MF_00163. Pep_deformylase. [Tree] |
| InterPro | IPR000181. Fmet_deformylase. IPR023635. Peptide_deformylase. [Graphical view] |
| Gene3D | G3DSA:3.90.45.10. Fmet_deformylase. 1 hit. |
| KO | K01462. |
| PANTHER | PTHR10458. Fmet_deformylase. 1 hit. |
| Pfam | PF01327. Pep_deformylase. 1 hit. [Graphical view] |
| PIRSF | PIRSF004749. Pep_def. 1 hit. |
| PRINTS | PR01576. PDEFORMYLASE. |
| SUPFAM | SSF56420. Fmet_deformylase. 1 hit. |
| TIGRFAMs | TIGR00079. Pept_deformyl. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | DEF_STRPS | ||||||||
| Accession | Primary (citable) accession number: B2IQS1 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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