ID   DEF2_RICCN              Reviewed;         202 AA.
AC   Q92JI7;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2002, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Peptide deformylase 2 {ECO:0000255|HAMAP-Rule:MF_00163};
DE            Short=PDF 2 {ECO:0000255|HAMAP-Rule:MF_00163};
DE            EC=3.5.1.88 {ECO:0000255|HAMAP-Rule:MF_00163};
DE   AltName: Full=Polypeptide deformylase 2 {ECO:0000255|HAMAP-Rule:MF_00163};
GN   Name=def2 {ECO:0000255|HAMAP-Rule:MF_00163}; OrderedLocusNames=RC0080;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(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.
CC       {ECO:0000255|HAMAP-Rule:MF_00163}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00163};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00163};
CC       Note=Binds 1 Fe(2+) ion. {ECO:0000255|HAMAP-Rule:MF_00163};
CC   -!- SIMILARITY: Belongs to the polypeptide deformylase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00163}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL02618.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE006914; AAL02618.1; ALT_INIT; Genomic_DNA.
DR   PIR; H97709; H97709.
DR   AlphaFoldDB; Q92JI7; -.
DR   SMR; Q92JI7; -.
DR   EnsemblBacteria; AAL02618; AAL02618; RC0080.
DR   KEGG; rco:RC0080; -.
DR   HOGENOM; CLU_061901_5_2_5; -.
DR   OMA; HREYSSV; -.
DR   Proteomes; UP000000816; 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   PIRSF; PIRSF004749; Pep_def; 1.
DR   PRINTS; PR01576; PDEFORMYLASE.
DR   SUPFAM; SSF56420; SSF56420; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Iron; Metal-binding; Protein biosynthesis.
FT   CHAIN           1..202
FT                   /note="Peptide deformylase 2"
FT                   /id="PRO_0000082830"
FT   ACT_SITE        163
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00163"
FT   BINDING         120
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00163"
FT   BINDING         162
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00163"
FT   BINDING         166
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00163"
SQ   SEQUENCE   202 AA;  23191 MW;  9A108195359D1B82 CRC64;
     MKNENNISLP QYVTLNIQTL NSSEDKTIRI KAKTLNFPLS SEDLRDISIL EKKYDQEENC
     AGLAAPQIGI SKCIIIFAVH EDAELKKWHP DLKDTMPKTI WINPSYKPIG IDKHEDYEGC
     FSVENATGPV ARFKKIHYHA YDINGNQIQG IAEGFLARVI QHEIDHLNGK VFLDYVAPKK
     IMTKEEYLEM RKKAMEQENI KS