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   25-MAY-2022, entry version 91.
DE   RecName: Full=Peptidyl-tRNA hydrolase 2 {ECO:0000255|HAMAP-Rule:MF_00083};
DE            Short=PTH 2 {ECO:0000255|HAMAP-Rule:MF_00083};
DE            EC=3.1.1.29 {ECO:0000255|HAMAP-Rule:MF_00083};
GN   Name=pth2 {ECO:0000255|HAMAP-Rule:MF_00083}; OrderedLocusNames=jk1496;
OS   Corynebacterium jeikeium (strain K411).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=306537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K411;
RX   PubMed=15968079; DOI=10.1128/jb.187.13.4671-4682.2005;
RA   Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA   Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA   Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT   "Complete genome sequence and analysis of the multiresistant nosocomial
RT   pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT   human skin flora.";
RL   J. Bacteriol. 187:4671-4682(2005).
CC   -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs
CC       which drop off the ribosome during protein synthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00083}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-
CC         amino acid + H(+); Xref=Rhea:RHEA:54448, Rhea:RHEA-COMP:10123,
CC         Rhea:RHEA-COMP:13883, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:59874, ChEBI:CHEBI:78442, ChEBI:CHEBI:138191;
CC         EC=3.1.1.29; Evidence={ECO:0000255|HAMAP-Rule:MF_00083};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00083}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00083}.
CC   -!- SIMILARITY: Belongs to the PTH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00083}.
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DR   EMBL; CR931997; CAI37669.1; -; Genomic_DNA.
DR   RefSeq; WP_005293388.1; NC_007164.1.
DR   AlphaFoldDB; Q4JU38; -.
DR   SMR; Q4JU38; -.
DR   STRING; 306537.jk1496; -.
DR   EnsemblBacteria; CAI37669; CAI37669; jk1496.
DR   GeneID; 56649154; -.
DR   KEGG; cjk:jk1496; -.
DR   eggNOG; COG0193; Bacteria.
DR   HOGENOM; CLU_062456_4_0_11; -.
DR   OMA; SQWLGTR; -.
DR   OrthoDB; 1676462at2; -.
DR   Proteomes; UP000000545; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00462; PTH; 1.
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   InterPro; IPR036416; Pept_tRNA_hydro_sf.
DR   PANTHER; PTHR17224; PTHR17224; 1.
DR   Pfam; PF01195; Pept_tRNA_hydro; 1.
DR   SUPFAM; SSF53178; SSF53178; 1.
DR   TIGRFAMs; TIGR00447; pth; 1.
DR   PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN           1..240
FT                   /note="Peptidyl-tRNA hydrolase 2"
FT                   /id="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