ID   DEFL_BRUSU              Reviewed;         164 AA.
AC   P63920; G0KCI9; Q8YBS4;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=Peptide deformylase-like;
DE   AltName: Full=Polypeptide deformylase-like;
GN   Name=def; OrderedLocusNames=BRA0454, BS1330_II0451;
OS   Brucella suis biovar 1 (strain 1330).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=204722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA   Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA   Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between animal
RT   and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=22038969; DOI=10.1128/jb.06181-11;
RA   Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT   "Revised genome sequence of Brucella suis 1330.";
RL   J. Bacteriol. 193:6410-6410(2011).
CC   -!- SIMILARITY: Belongs to the polypeptide deformylase family.
CC       {ECO:0000305}.
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DR   EMBL; AE014292; AAN33648.1; -; Genomic_DNA.
DR   EMBL; CP002998; AEM19927.1; -; Genomic_DNA.
DR   AlphaFoldDB; P63920; -.
DR   SMR; P63920; -.
DR   KEGG; bms:BRA0454; -.
DR   KEGG; bsi:BS1330_II0451; -.
DR   PATRIC; fig|204722.22.peg.3241; -.
DR   HOGENOM; CLU_061901_2_0_5; -.
DR   Proteomes; UP000007104; Chromosome II.
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; Peptide deformylase; 1.
DR   HAMAP; MF_00163; Pep_deformylase; 1.
DR   InterPro; IPR023635; Peptide_deformylase.
DR   InterPro; IPR036821; Peptide_deformylase_sf.
DR   NCBIfam; TIGR00079; pept_deformyl; 1.
DR   PANTHER; PTHR10458; PEPTIDE DEFORMYLASE; 1.
DR   PANTHER; PTHR10458:SF22; PEPTIDE DEFORMYLASE; 1.
DR   Pfam; PF01327; Pep_deformylase; 1.
DR   PIRSF; PIRSF004749; Pep_def; 1.
DR   PRINTS; PR01576; PDEFORMYLASE.
DR   SUPFAM; SSF56420; Peptide deformylase; 1.
PE   3: Inferred from homology;
FT   CHAIN           1..164
FT                   /note="Peptide deformylase-like"
FT                   /id="PRO_0000082893"
FT   ACT_SITE        134
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   164 AA;  18857 MW;  BA2B8C3F9C4E766C CRC64;
     MTVRLIVKYP DPRLRAAAEP VTTFDEGLRK LADDLLDTMR AAPGIGITAP HIGISKRVVV
     LELDRAAGPK IYINPEIVWA CEEKIRHQEG SVSMPGVVDE VERHARIRLR YQDLDGNEQT
     EESDGLLAVC HQHEIDQLDG IFWVQRLSRL RRERLIKRYE KLQR
//