ID   DEF_STAAU               Reviewed;         183 AA.
AC   P68826; Q9F4L4;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-NOV-2008, entry version 28.
DE   RecName: Full=Peptide deformylase;
DE            Short=PDF;
DE            EC=3.5.1.88;
DE   AltName: Full=Polypeptide deformylase;
GN   Name=def; Synonyms=def1, pdf1;
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WCUH29 / NCIMB 40771;
RA   Lonetto M.A., Sylvester D.R., Warren R.L.;
RT   "Staphylococcus aureus deformylase 1 encoding DNA.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   MASS SPECTROMETRY.
RC   STRAIN=MRSA-M2;
RX   PubMed=16714572; DOI=10.1128/IAI.00392-06;
RA   Brady R.A., Leid J.G., Camper A.K., Costerton J.W., Shirtliff M.E.;
RT   "Identification of Staphylococcus aureus proteins recognized by the
RT   antibody-mediated immune response to a biofilm infection.";
RL   Infect. Immun. 74:3415-3426(2006).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
RX   PubMed=12823970; DOI=10.1016/S0022-2836(03)00596-5;
RA   Kreusch A., Spraggon G., Lee C.C., Klock H., McMullan D., Ng K.,
RA   Shin T., Vincent J., Warner I., Ericson C., Lesley S.A.;
RT   "Structure analysis of peptide deformylases from Streptococcus
RT   pneumoniae, Staphylococcus aureus, Thermotoga maritima and Pseudomonas
RT   aeruginosa: snapshots of the oxygen sensitivity of peptide
RT   deformylase.";
RL   J. Mol. Biol. 330:309-321(2003).
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: Formyl-L-methionyl peptide + H(2)O = formate +
CC       methionyl peptide.
CC   -!- COFACTOR: Binds 1 Fe(2+) ion (By similarity).
CC   -!- MASS SPECTROMETRY: Mass=20600; Method=MALDI; Range=1-183;
CC       Source=PubMed:16714572;
CC   -!- SIMILARITY: Belongs to the polypeptide deformylase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY007227; AAG02249.1; -; Genomic_DNA.
DR   PDB; 1LM4; X-ray; 1.45 A; A/B=1-183.
DR   PDB; 1LMH; X-ray; 1.90 A; A=1-183.
DR   PDB; 1LQW; X-ray; 1.87 A; A/B=1-183.
DR   PDB; 1Q1Y; X-ray; 1.90 A; A=1-183.
DR   PDB; 2AI9; X-ray; 2.50 A; A/B=1-183.
DR   PDBsum; 1LM4; -.
DR   PDBsum; 1LMH; -.
DR   PDBsum; 1LQW; -.
DR   PDBsum; 1Q1Y; -.
DR   PDBsum; 2AI9; -.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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    183       Peptide deformylase.
FT                                /FTId=PRO_0000082843.
FT   ACT_SITE    155    155       By similarity.
FT   METAL       111    111       Iron.
FT   METAL       154    154       Iron.
FT   METAL       158    158       Iron.
FT   HELIX         4      6
FT   HELIX        13     16
FT   HELIX        28     45
FT   HELIX        47     53
FT   STRAND       58     62
FT   HELIX        63     66
FT   STRAND       70     77
FT   STRAND       81     83
FT   STRAND       86     98
FT   STRAND      100    104
FT   STRAND      124    133
FT   STRAND      139    145
FT   HELIX       146    159
FT   HELIX       164    167
FT   STRAND      170    172
SQ   SEQUENCE   183 AA;  20559 MW;  32A64066A6FEAB0E CRC64;
     MLTMKDIIRD GHPTLRQKAA ELELPLTKEE KETLIAMREF LVNSQDEEIA KRYGLRSGVG
     LAAPQINISK RMIAVLIPDD GSGKSYDYML VNPKIVSHSV QEAYLPTGEG CLSVDDNVAG
     LVHRHNRITI KAKDIEGNDI QLRLKGYPAI VFQHEIDHLN GVMFYDHIDK NHPLQPHTDA
     VEV
//