ID   DEF_LACLA               Reviewed;         196 AA.
AC   Q48661; Q9CI08;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 3.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Peptide deformylase;
DE            Short=PDF;
DE            EC=3.5.1.88;
DE   AltName: Full=Polypeptide deformylase;
GN   Name=def; OrderedLocusNames=LL0560; ORFNames=L154885;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LM0230;
RX   PubMed=7773380; DOI=10.1099/13500872-141-4-1027;
RA   Cancilla M.R., Hillier A.J., Davidson B.E.;
RT   "Lactococcus lactis glyceraldehyde-3-phosphate dehydrogenase gene, gap:
RT   further evidence for strongly biased codon usage in glycolytic pathway
RT   genes.";
RL   Microbiology 141:1027-1036(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
CC   -!- FUNCTION: Removes the formyl group from the N-terminal Met of newly
CC       synthesized proteins. Requires at least a dipeptide for an efficient
CC       rate of reaction. N-terminal L-methionine is a prerequisite for
CC       activity but the enzyme has broad specificity at other positions (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-terminal N-formyl-L-methionyl-[peptide] = formate + N-
CC         terminal L-methionyl-[peptide]; Xref=Rhea:RHEA:24420, Rhea:RHEA-
CC         COMP:10639, Rhea:RHEA-COMP:10640, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:49298, ChEBI:CHEBI:64731; EC=3.5.1.88;
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe(2+) ion. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the polypeptide deformylase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC41454.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAK04658.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L36907; AAC41454.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AE005176; AAK04658.1; ALT_INIT; Genomic_DNA.
DR   PIR; H86694; H86694.
DR   RefSeq; NP_266716.1; NC_002662.1.
DR   AlphaFoldDB; Q48661; -.
DR   SMR; Q48661; -.
DR   STRING; 272623.L154885; -.
DR   PaxDb; Q48661; -.
DR   EnsemblBacteria; AAK04658; AAK04658; L154885.
DR   KEGG; lla:L154885; -.
DR   PATRIC; fig|272623.7.peg.598; -.
DR   eggNOG; COG0242; Bacteria.
DR   HOGENOM; CLU_061901_4_0_9; -.
DR   OMA; DMMEYLV; -.
DR   Proteomes; UP000002196; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042586; F:peptide deformylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00487; Pep_deformylase; 1.
DR   Gene3D; 3.90.45.10; -; 1.
DR   HAMAP; MF_00163; Pep_deformylase; 1.
DR   InterPro; IPR023635; Peptide_deformylase.
DR   InterPro; IPR036821; Peptide_deformylase_sf.
DR   PANTHER; PTHR10458; PTHR10458; 1.
DR   Pfam; PF01327; Pep_deformylase; 1.
DR   PRINTS; PR01576; PDEFORMYLASE.
DR   SUPFAM; SSF56420; SSF56420; 1.
DR   TIGRFAMs; TIGR00079; pept_deformyl; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Iron; Metal-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..196
FT                   /note="Peptide deformylase"
FT                   /id="PRO_0000082792"
FT   ACT_SITE        167
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        86
FT                   /note="D -> E (in Ref. 1; AAC41454)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   196 AA;  22047 MW;  C5914BB3A92BF243 CRC64;
     MISMDDIIRE GYPTLREVAN DVTLPLSDED IILGEKMLQF LHNSQDPVMA EKMGLRGGVG
     LAANQLGLLK KVIAVLIPNE PEVDEDGNEI PPKEAYKMRE IMYNAKVVSH SVQDAAVEGG
     EGCLSVDREV PGYVVRHARV TVEYYNKEGE KKKIRLKDFP AICVQHEIDH TNGVMFYDHI
     NMNDPWEIKD GMIIVK