ID   PTH_CUPMC               Reviewed;         198 AA.
AC   Q1LRQ3;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000255|HAMAP-Rule:MF_00083};
DE            Short=PTH {ECO:0000255|HAMAP-Rule:MF_00083};
DE            EC=3.1.1.29 {ECO:0000255|HAMAP-Rule:MF_00083};
GN   Name=pth {ECO:0000255|HAMAP-Rule:MF_00083}; OrderedLocusNames=Rmet_0287;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
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; CP000352; ABF07173.1; -; Genomic_DNA.
DR   RefSeq; WP_011515176.1; NC_007973.1.
DR   AlphaFoldDB; Q1LRQ3; -.
DR   SMR; Q1LRQ3; -.
DR   STRING; 266264.Rmet_0287; -.
DR   EnsemblBacteria; ABF07173; ABF07173; Rmet_0287.
DR   KEGG; rme:Rmet_0287; -.
DR   eggNOG; COG0193; Bacteria.
DR   HOGENOM; CLU_062456_3_1_4; -.
DR   OMA; HVLSKFH; -.
DR   OrthoDB; 1676462at2; -.
DR   Proteomes; UP000002429; 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; PS01195; PEPT_TRNA_HYDROL_1; 1.
DR   PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN           1..198
FT                   /note="Peptidyl-tRNA hydrolase"
FT                   /id="PRO_0000264086"
SQ   SEQUENCE   198 AA;  21630 MW;  D322466EF2CBEB36 CRC64;
     MIKLIVGLGN PGAEYEATRH NAGFWLVDQL ARMGGTTLRV ESRFHGLAGR ARLWDQDVWL
     LKPSTFMNRS GLSVVSLARF YKILPDEIVV AHDEMDLPAG SAKLKRGGGS GGHNGLKDIS
     AHLTTQDYWR LRIGVGHPRN APGGAAGGRE DVVNFVLKPP RKEEQQAIDE AIDRCIGPLG
     TLARGESERA MMELHTGR