ID   DEF2_BACST              Reviewed;         184 AA.
AC   O31410;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 61.
DE   RecName: Full=Peptide deformylase 2;
DE            Short=PDF 2;
DE            EC=3.5.1.88;
DE   AltName: Full=Polypeptide deformylase 2;
OS   Bacillus stearothermophilus (Geobacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=ATCC 1518;
RX   MEDLINE=97272005; PubMed=9126850; DOI=10.1006/jmbi.1997.0904;
RA   Meinnel T., Lazennec C., Villoing S., Blanquet S.;
RT   "Structure-function relationships within the peptide deformylase
RT   family. Evidence for a conserved architecture of the active site
RT   involving three conserved motifs and a metal ion.";
RL   J. Mol. Biol. 267:749-761(1997).
CC   -!- FUNCTION: Removes the formyl group from the N-terminal Met of
CC       newly synthesized proteins. Requires at least a dipeptide for an
CC       efficient rate of reaction. N-terminal L-methionine is a
CC       prerequisite for activity but the enzyme has broad specificity at
CC       other positions.
CC   -!- CATALYTIC ACTIVITY: Formyl-L-methionyl peptide + H(2)O = formate +
CC       methionyl peptide.
CC   -!- COFACTOR: Binds 1 Fe(2+) ion (By similarity).
CC   -!- SIMILARITY: Belongs to the polypeptide deformylase family.
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DR   EMBL; Y10549; CAA71581.1; -; Genomic_DNA.
DR   PDB; 1LQY; X-ray; 1.90 A; A=1-184.
DR   PDBsum; 1LQY; -.
DR   BRENDA; 3.5.1.88; 266715.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042586; F:peptide deformylase activity; IEA:HAMAP.
DR   GO; GO:0006412; P:translation; IEA:HAMAP.
DR   HAMAP; MF_00163; -; 1.
DR   InterPro; IPR000181; Fmet_deformylase.
DR   Gene3D; G3DSA:3.90.45.10; Fmet_deformylase; 1.
DR   PANTHER; PTHR10458; Fmet_deformylase; 1.
DR   Pfam; PF01327; Pep_deformylase; 1.
DR   PIRSF; PIRSF004749; Pep_def; 1.
DR   PRINTS; PR01576; PDEFORMYLASE.
DR   ProDom; PD003844; Fmet_deformylase; 1.
DR   TIGRFAMs; TIGR00079; pept_deformyl; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Hydrolase; Iron; Metal-binding; Protein biosynthesis.
FT   CHAIN         1    184       Peptide deformylase 2.
FT                                /FTId=PRO_0000082738.
FT   ACT_SITE    154    154       By similarity.
FT   METAL       110    110       Iron (By similarity).
FT   METAL       153    153       Iron (By similarity).
FT   METAL       157    157       Iron (By similarity).
FT   HELIX         4      6
FT   HELIX        13     16
FT   HELIX        28     44
FT   HELIX        47     53
FT   STRAND       59     62
FT   HELIX        63     66
FT   STRAND       70     78
FT   STRAND       84     97
FT   STRAND       99    104
FT   STRAND      123    132
FT   STRAND      138    144
FT   HELIX       145    158
FT   HELIX       163    166
FT   STRAND      180    182
SQ   SEQUENCE   184 AA;  20383 MW;  9CD85DEE53632FA0 CRC64;
     MITMKDIIKE GHPTLRKVAE PVPLPPSEED KRILQSLLDY VKMSQDPELA AKYGLRPGIG
     LAAPQINVSK RMIAVHVTDE NGTLYSYALF NPKIVSHSVQ QCYLTTGEGC LSVDRDVPGY
     VLRYARITVT GTTLDGEEVT LRLKGLPAIV FQHEIDHLNG IMFYDRINPA DPFQVPDGAI
     PIGR
//