ID   PTH_BORA1               Reviewed;         207 AA.
AC   Q2KY99;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Peptidyl-tRNA hydrolase;
DE            Short=PTH;
DE            EC=3.1.1.29;
GN   Name=pth; OrderedLocusNames=BAV0539;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
CC   -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-
CC       tRNAs which drop off the ribosome during protein synthesis (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: N-substituted aminoacyl-tRNA + H(2)O = N-
CC       substituted amino acid + tRNA.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the PTH family.
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DR   EMBL; AM167904; CAJ48144.1; -; Genomic_DNA.
DR   RefSeq; YP_785072.1; -.
DR   GeneID; 6267695; -.
DR   GenomeReviews; AM167904_GR; BAV0539.
DR   KEGG; bav:BAV0539; -.
DR   NMPDR; fig|521.1.peg.1019; -.
DR   HOGENOM; Q2KY99; -.
DR   OMA; Q2KY99; KIPLDNI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA:HAMAP.
DR   GO; GO:0006412; P:translation; IEA:HAMAP.
DR   HAMAP; MF_00083; -; 1.
DR   InterPro; IPR001328; Pept_tRNA_hydro.
DR   InterPro; IPR018171; Pept_tRNA_hydro_CS.
DR   Gene3D; G3DSA:3.40.50.1470; Pept_tRNA_hydro; 1.
DR   PANTHER; PTHR17224; Pept_tRNA_hydro; 1.
DR   Pfam; PF01195; Pept_tRNA_hydro; 1.
DR   ProDom; PD005324; PeptRNAhydrolase; 1.
DR   TIGRFAMs; TIGR00447; pth; 1.
DR   PROSITE; PS01195; PEPT_TRNA_HYDROL_1; 1.
DR   PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Hydrolase.
FT   CHAIN         1    207       Peptidyl-tRNA hydrolase.
FT                                /FTId=PRO_0000264008.
SQ   SEQUENCE   207 AA;  22831 MW;  A1493C67267256B0 CRC64;
     MHAQGFLCSK HAMSEPIRLI VGLGNPGPDY ETTRHNAGFW LADRLADDLR ATFALEKGFM
     GMVAKARFEG ENVLLLKPIT YMNRSGQAVG ALARFYKLAP EQVLVLHDEL DLLPGQVKMK
     QGGGHAGHNG LKDIQAALGT PNFWRLRLGI GHPRTLNLAQ QVADFVLHPP RRDEQAEIDT
     VIDRCRAVVP ALLRGDFAQA TRQLHTA
//