ID   PTH2_CORJK              Reviewed;         240 AA.
AC   Q4JU38;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=Peptidyl-tRNA hydrolase 2;
DE            Short=PTH 2;
DE            EC=3.1.1.29;
GN   Name=pth2; OrderedLocusNames=jk1496;
OS   Corynebacterium jeikeium (strain K411).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=306537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005;
RA   Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B.,
RA   Albersmeier A., Bekel T., Bischoff N., Brune I., Chakraborty T.,
RA   Kalinowski J., Meyer F., Rupp O., Schneiker S., Viehoever P.,
RA   Puehler A.;
RT   "Complete genome sequence and analysis of the multiresistant
RT   nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring
RT   bacterium of the human skin flora.";
RL   J. Bacteriol. 187:4671-4682(2005).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CR931997; CAI37669.1; -; Genomic_DNA.
DR   RefSeq; YP_251287.1; -.
DR   GeneID; 3432995; -.
DR   GenomeReviews; CR931997_GR; jk1496.
DR   KEGG; cjk:jk1496; -.
DR   NMPDR; fig|306537.3.peg.749; -.
DR   HOGENOM; Q4JU38; -.
DR   OMA; Q4JU38; IARNDIH.
DR   BioCyc; CJEI306537:JK1496-MON; -.
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; FALSE_NEG.
DR   PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Hydrolase.
FT   CHAIN         1    240       Peptidyl-tRNA hydrolase 2.
FT                                /FTId=PRO_0000264026.
SQ   SEQUENCE   240 AA;  26242 MW;  5FACA1DD8B825B7C CRC64;
     MAVSFLQSLF SVFRKKSSPQ EPATTTAGGP AKRTKLTVGE LQEFAPEWIV IGLGNPGAKY
     ADTRHNIGYW PIDRLVERYE AQWLPVEGQK AHAALITVEE TPVLLLRSTT YMNNSGEAVG
     PLASALSLPA ERIIVCHDEL DIAAGQVRIK DKGGEGGHNG LRSMTAELGT QHYVRVRMGI
     GRPPKGTSVI DFVLSPFEEA DIDAENGWME NTLRDSVDSV TLIVNNGTDI ARNDIHTRKH
//