ID   PTH_RHOPT               Reviewed;         206 AA.
AC   B3Q7X3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=Rpal_4839;
OS   Rhodopseudomonas palustris (strain TIE-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=395960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TIE-1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA   Newman D.K., Roden E., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001096; ACF03328.1; -; Genomic_DNA.
DR   RefSeq; WP_011159889.1; NC_011004.1.
DR   AlphaFoldDB; B3Q7X3; -.
DR   SMR; B3Q7X3; -.
DR   EnsemblBacteria; ACF03328; ACF03328; Rpal_4839.
DR   GeneID; 66895488; -.
DR   KEGG; rpt:Rpal_4839; -.
DR   HOGENOM; CLU_062456_1_0_5; -.
DR   OMA; HVLSKFH; -.
DR   OrthoDB; 1676462at2; -.
DR   BioCyc; RPAL395960:RPAL_RS23935-MON; -.
DR   Proteomes; UP000001725; 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.
FT   CHAIN           1..206
FT                   /note="Peptidyl-tRNA hydrolase"
FT                   /id="PRO_1000092977"
SQ   SEQUENCE   206 AA;  22568 MW;  9CA48853ACFCA4F8 CRC64;
     MRLFVGLGNP GAKYQGNRHN IGFMVIDEIA RRHGFSPWRR RFQGETADGV LDGERITLLK
     PLTYMNESGR AVQDAASFYK IGQNEIAVFH DEIELPPAKV RVKVGGGIAG HNGLRSISAH
     IGNDYLRVRL GVGHPGAKEL VHNHVLGDFA KSERPWVEAL CEIAADNAGL IAKGKDASFA
     NKVHLAMQAK GFYDNDKQAK GGERDK