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PTH_BURM1
ID   PTH_BURM1               Reviewed;         199 AA.
AC   A9AEY6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 87.
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};
GN   OrderedLocusNames=Bmul_0511, BMULJ_02749;
OS   Burkholderia multivorans (strain ATCC 17616 / 249).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=395019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC
RT   17616.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA   Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA   Hattori M., Tsuda M.;
RT   "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL   Submitted (APR-2007) 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; CP000868; ABX14206.1; -; Genomic_DNA.
DR   EMBL; AP009385; BAG44637.1; -; Genomic_DNA.
DR   RefSeq; WP_006398241.1; NC_010804.1.
DR   AlphaFoldDB; A9AEY6; -.
DR   SMR; A9AEY6; -.
DR   STRING; 395019.Bmul_0511; -.
DR   EnsemblBacteria; BAG44637; BAG44637; BMULJ_02749.
DR   KEGG; bmj:BMULJ_02749; -.
DR   KEGG; bmu:Bmul_0511; -.
DR   eggNOG; COG0193; Bacteria.
DR   HOGENOM; CLU_062456_3_1_4; -.
DR   OMA; HVLSKFH; -.
DR   Proteomes; UP000008815; Chromosome 1.
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..199
FT                   /note="Peptidyl-tRNA hydrolase"
FT                   /id="PRO_1000092919"
SQ   SEQUENCE   199 AA;  22055 MW;  7BB331F801FD24A3 CRC64;
     MIKLIVGLGN PGAEYTATRH NAGFWLIDQL AREAGATLRD ERRFHGFYAK ARLYGEEVHL
     LEPQTYMNRS GQSVVALAHF FKILPDQILV AHDELDLPPG TVKLKLGGGS GGHNGLKDIS
     AHLSSQQYWR LRIGIGHPRD LIPESARAGA KPDVANFVLK PPRREEQDVI DAAIERALAV
     MPMVVKGELD RATMQLHRN
 
 
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