DEFL_BRUSU
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 25-MAY-2022, entry version 83.
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; Proteobacteria; 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 RefSeq; WP_002966173.1; NZ_KN046805.1.
DR AlphaFoldDB; P63920; -.
DR SMR; P63920; -.
DR EnsemblBacteria; AEM19927; AEM19927; BS1330_II0451.
DR GeneID; 45053506; -.
DR KEGG; bms:BRA0454; -.
DR KEGG; bsi:BS1330_II0451; -.
DR PATRIC; fig|204722.22.peg.3241; -.
DR HOGENOM; CLU_061901_2_0_5; -.
DR OMA; NMHGEPV; -.
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; -; 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.
DR TIGRFAMs; TIGR00079; pept_deformyl; 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