P99077 (DEF_STAAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 58.
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 | Staphylococcus aureus (strain N315) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 158879 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus › ![]() |
Protein attributes
| Sequence length | 183 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
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-Rule MF_00163 |
| Catalytic activity | Formyl-L-methionyl peptide + H2O = formate + methionyl peptide. HAMAP-Rule MF_00163 |
| Cofactor | Binds 1 Fe2+ ion By similarity. |
| 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: HAMAP |
| Molecular_function | iron ion binding Inferred from electronic annotation. Source: InterPro peptide deformylase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 183 | 183 | Peptide deformylase HAMAP-Rule MF_00163 | PRO_0000082840 | |||||
Sites | |||||||||
| Active site | 155 | 1 | By similarity | ||||||
| Metal binding | 111 | 1 | Iron By similarity | ||||||
| Metal binding | 154 | 1 | Iron By similarity | ||||||
| Metal binding | 158 | 1 | Iron By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. Hiramatsu K.Lancet 357:1225-1240(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: N315. |
| [2] | "Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth." Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J. J. Microbiol. Methods 60:247-257(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY. Strain: N315. |
| [3] | "Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315." Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F. Submitted (OCT-2007) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: N315. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000018 Genomic DNA. Translation: BAB42188.1. |
| PIR | A89879. |
| RefSeq | NP_374210.1. NC_002745.2. |
3D structure databases | |
| ProteinModelPortal | P99077. |
| SMR | P99077. Positions 1-183. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 158879.SA0942. |
2D gel databases | |
| SWISS-2DPAGE | P99077. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAB42188; BAB42188; BAB42188. |
| GeneID | 1123766. |
| KEGG | sau:SA0942. |
| PATRIC | 19574074. VBIStaAur116463_1007. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0242. |
| HOGENOM | HOG000243507. |
| KO | K01462. |
| OMA | LTSGEGC. |
| ProtClustDB | PRK00150. |
Enzyme and pathway databases | |
| BioCyc | SAUR158879:GJCB-995-MONOMER. |
Family and domain databases | |
| Gene3D | 3.90.45.10. 1 hit. |
| HAMAP | MF_00163. Pep_deformylase. |
| InterPro | IPR000181. Fmet_deformylase. IPR023635. Peptide_deformylase. [Graphical view] |
| PANTHER | PTHR10458. PTHR10458. 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... |
Other | |
| BindingDB | P99077. |
Entry information
| Entry name | DEF_STAAN | ||||||||
| Accession | Primary (citable) accession number: P99077 Secondary accession number(s): Q9F4L4 | ||||||||
| 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 |

Clusters with
