ID   PTH_PORG3               Reviewed;         185 AA.
AC   B2RHF2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=PGN_0278;
OS   Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS   12257 / NCTC 11834 / 2561).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=431947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561;
RX   PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA   Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA   Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA   Nakayama K.;
RT   "Determination of the genome sequence of Porphyromonas gingivalis strain
RT   ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT   rearrangements in P. gingivalis.";
RL   DNA Res. 15:215-225(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP009380; BAG32797.1; -; Genomic_DNA.
DR   RefSeq; WP_012457388.1; NZ_CP025930.1.
DR   AlphaFoldDB; B2RHF2; -.
DR   SMR; B2RHF2; -.
DR   STRING; 431947.PGN_0278; -.
DR   EnsemblBacteria; BAG32797; BAG32797; PGN_0278.
DR   GeneID; 29255526; -.
DR   KEGG; pgn:PGN_0278; -.
DR   eggNOG; COG0193; Bacteria.
DR   HOGENOM; CLU_062456_4_1_10; -.
DR   OMA; HVLSKFH; -.
DR   BioCyc; PGIN431947:G1G2V-305-MON; -.
DR   Proteomes; UP000008842; 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..185
FT                   /note="Peptidyl-tRNA hydrolase"
FT                   /id="PRO_1000092969"
SQ   SEQUENCE   185 AA;  20744 MW;  65F314EBF0BE7A14 CRC64;
     MKYLIVGLGN IGGEYNGTRH NVGFRMVNAL AEDGGVQFVE ARYGAIAHMR VKNAELILLK
     PNTYMNLSGN AVRYWMQQEN IPREQVLVLV DDLALPFGTL RLKPKGSDAG HNGLKNIAEV
     MGSIDYARLR FGLGDEFSKG RQVDFVLGRF TPEEEEKLPE LTKHAVEIIK SFCLAGIQRT
     MNRYN