ID   PTH_AGRRK               Reviewed;         238 AA.
AC   B9J795;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   29-MAY-2013, entry version 32.
DE   RecName: Full=Peptidyl-tRNA hydrolase;
DE            Short=PTH;
DE            EC=3.1.1.29;
GN   Name=pth; OrderedLocusNames=Arad_3192;
OS   Agrobacterium radiobacter (strain K84 / ATCC BAA-868).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=311403;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K84 / ATCC BAA-868;
RX   PubMed=19251847; DOI=10.1128/JB.01779-08;
RA   Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K.,
RA   Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I.,
RA   Otten L., Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T.,
RA   Du Z., Ewing A., Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J.,
RA   Miller N.M., Norton S., Chen Q., Phoolcharoen W., Ohlin V.,
RA   Ondrusek D., Pride N., Stricklin S.L., Sun J., Wheeler C., Wilson L.,
RA   Zhu H., Wood D.W.;
RT   "Genome sequences of three Agrobacterium biovars help elucidate the
RT   evolution of multichromosome genomes in bacteria.";
RL   J. Bacteriol. 191:2501-2511(2009).
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; CP000628; ACM27202.1; -; Genomic_DNA.
DR   RefSeq; YP_002545132.1; NC_011985.1.
DR   STRING; 311403.Arad_3192; -.
DR   EnsemblBacteria; ACM27202; ACM27202; Arad_3192.
DR   GeneID; 7370806; -.
DR   KEGG; ara:Arad_3192; -.
DR   PATRIC; 20805805; VBIAgrRad129173_4983.
DR   eggNOG; COG0193; -.
DR   HOGENOM; HOG000004797; -.
DR   KO; K01056; -.
DR   OMA; KPETFMN; -.
DR   ProtClustDB; PRK05426; -.
DR   BioCyc; ARAD311403:GHU8-2476-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA:EC.
DR   Gene3D; 3.40.50.1470; -; 1.
DR   HAMAP; MF_00083; Pept_tRNA_hydro_bact; 1; -.
DR   InterPro; IPR001328; Pept_tRNA_hydro.
DR   InterPro; IPR018171; Pept_tRNA_hydro_CS.
DR   PANTHER; PTHR17224; PTHR17224; 1.
DR   Pfam; PF01195; Pept_tRNA_hydro; 1.
DR   SUPFAM; SSF53178; Pept_tRNA_hydro; 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    238       Peptidyl-tRNA hydrolase.
FT                                /FTId=PRO_1000192952.
SQ   SEQUENCE   238 AA;  26358 MW;  8E1E07C67FB4CF32 CRC64;
     MLLIVGLGNP GAKYQGNRHN IGFMAVDAIH RRHSFSPWAK KFRAEISEGE LGGQKVLLIK
     PQTFMNLSGE SVGEAMRFYK LEPSDLVVIY DELDLPAAKA RLKTGGGHGG HNGIKSIDAH
     CGREYRRLRL GIGHPGVKEL VQNHVLGDFA KVDRDWLEPL FDALADNADM LVRGEDSQLM
     NKIALALGGK TEEPAPKPEK KTVAKSHIHQ ARNHNQPRMP ESGPMAEMLK RMFGKKDD
//