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Q0SS77 (Q0SS77_CLOPS) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peptide deformylase 2 HAMAP MF_00163
Short name=PDF 2 HAMAP MF_00163
EC=3.5.1.88 HAMAP MF_00163
Alternative name(s):
Polypeptide deformylase 2 HAMAP MF_00163
Gene names
Name:def_2 EMBL ABG86243.1
Synonyms:def2 HAMAP MF_00163
Ordered Locus Names:CPR_1715
OrganismClostridium perfringens (strain SM101 / Type A) [Complete proteome] [HAMAP] EMBL ABG86243.1
Taxonomic identifier289380 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length147 AA.
Sequence statusComplete.
Protein existenceInferred 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 SAAS SAAS000181

Cofactor

Binds 1 Fe2+ ion By similarity. HAMAP MF_00163

Sequence similarities

Belongs to the polypeptide deformylase family. HAMAP MF_00163

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1331 By similarity HAMAP MF_00163
Metal binding901Iron By similarity HAMAP MF_00163
Metal binding1321Iron By similarity HAMAP MF_00163
Metal binding1361Iron By similarity HAMAP MF_00163

Sequences

Sequence LengthMass (Da)Tools
Q0SS77 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 65DB01378010472C

FASTA14716,616
        10         20         30         40         50         60 
MAIRNLRFND DEILRKKCRV VDDINDRIKV LVEDMIETMY ENNGVGLASP QVGILKRIFV 

        70         80         90        100        110        120 
VDAMDGAGSR VFINPEILEK SGEQTDEEGC LSLPGRHKPV KRANKIKIKA LDVNGNEFVL 

       130        140 
DAEGFLARAI QHEYDHLEGV LFIDHEL

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000312 Genomic DNA. Translation: ABG86243.1.
RefSeqYP_699030.1. NC_008262.1.

3D structure databases

ProteinModelPortalQ0SS77.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0SS77.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4204622.
GenomeReviewsGene locus CPR_1715 in contig CP000312_GR.
KEGGcpr:CPR_1715.
PATRIC19491731. VBICloPer122123_1694.
TIGRCPR_1715.

Phylogenomic databases

eggNOGCOG0242.
HOGENOMHBG665227.
OMAGVLFVDY.
ProtClustDBPRK00150.

Family and domain databases

HAMAPMF_00163. Pep_deformylase.
[Tree]
InterProIPR000181. Fmet_deformylase.
IPR023635. Peptide_deformylase.
[Graphical view]
Gene3DG3DSA:3.90.45.10. Fmet_deformylase. 1 hit.
KOK01462.
PANTHERPTHR10458. Fmet_deformylase. 1 hit.
PfamPF01327. Pep_deformylase. 1 hit.
[Graphical view]
PIRSFPIRSF004749. Pep_def. 1 hit.
PRINTSPR01576. PDEFORMYLASE.
SUPFAMSSF56420. Fmet_deformylase. 1 hit.
TIGRFAMsTIGR00079. Pept_deformyl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ0SS77_CLOPS
AccessionPrimary (citable) accession number: Q0SS77
Entry history
Integrated into UniProtKB/TrEMBL: September 5, 2006
Last sequence update: September 5, 2006
Last modified: December 14, 2011
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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