ID   PTH_BURTA               Reviewed;         201 AA.
AC   Q2T1B9;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=BTH_I0472;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS   E264).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(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; CP000086; ABC37803.1; -; Genomic_DNA.
DR   RefSeq; WP_009893073.1; NZ_CP008785.1.
DR   PDB; 3V2I; X-ray; 1.65 A; A=1-201.
DR   PDBsum; 3V2I; -.
DR   AlphaFoldDB; Q2T1B9; -.
DR   SMR; Q2T1B9; -.
DR   PRIDE; Q2T1B9; -.
DR   EnsemblBacteria; ABC37803; ABC37803; BTH_I0472.
DR   GeneID; 66545998; -.
DR   KEGG; bte:BTH_I0472; -.
DR   HOGENOM; CLU_062456_3_1_4; -.
DR   OMA; HVLSKFH; -.
DR   OrthoDB; 1676462at2; -.
DR   Proteomes; UP000001930; Chromosome I.
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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Hydrolase.
FT   CHAIN           1..201
FT                   /note="Peptidyl-tRNA hydrolase"
FT                   /id="PRO_0000264014"
FT   STRAND          4..7
FT                   /evidence="ECO:0007829|PDB:3V2I"
FT   HELIX           13..15
FT                   /evidence="ECO:0007829|PDB:3V2I"
FT   HELIX           19..21
FT                   /evidence="ECO:0007829|PDB:3V2I"
FT   HELIX           22..34
FT                   /evidence="ECO:0007829|PDB:3V2I"
FT   STRAND          39..41
FT                   /evidence="ECO:0007829|PDB:3V2I"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:3V2I"
FT   STRAND          46..53
FT                   /evidence="ECO:0007829|PDB:3V2I"
FT   STRAND          56..63
FT                   /evidence="ECO:0007829|PDB:3V2I"
FT   HELIX           67..69
FT                   /evidence="ECO:0007829|PDB:3V2I"
FT   HELIX           70..81
FT                   /evidence="ECO:0007829|PDB:3V2I"
FT   HELIX           85..87
FT                   /evidence="ECO:0007829|PDB:3V2I"
FT   STRAND          88..94
FT                   /evidence="ECO:0007829|PDB:3V2I"
FT   STRAND          102..106
FT                   /evidence="ECO:0007829|PDB:3V2I"
FT   HELIX           114..123
FT                   /evidence="ECO:0007829|PDB:3V2I"
FT   STRAND          128..134
FT                   /evidence="ECO:0007829|PDB:3V2I"
FT   TURN            138..141
FT                   /evidence="ECO:0007829|PDB:3V2I"
FT   HELIX           154..157
FT                   /evidence="ECO:0007829|PDB:3V2I"
FT   HELIX           164..185
FT                   /evidence="ECO:0007829|PDB:3V2I"
FT   HELIX           189..195
FT                   /evidence="ECO:0007829|PDB:3V2I"
SQ   SEQUENCE   201 AA;  22101 MW;  DFC60EDEEA574DAC CRC64;
     MIKLIVGLGN PGAEYTATRH NAGFWLVDQL AREAGATLRD ERRFHGFYAK ARLYGEEVHL
     LEPQTYMNRS GQSVVALAHF FKILPNEILV AHDELDLPPG AVKLKLGGGS GGHNGLKDIS
     AHLSSQQYWR LRIGIGHPRD MIPESARAGA KPDVANFVLK PPRKEEQDVI DAAIERALAV
     MPAVVKGETE RAMMQLHRNG A