ID   PTH_STAAU               Reviewed;         190 AA.
AC   Q6YP15;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000255|HAMAP-Rule:MF_00083, ECO:0000303|PubMed:11812233};
DE            Short=PTH {ECO:0000255|HAMAP-Rule:MF_00083, ECO:0000303|PubMed:12069408};
DE            EC=3.1.1.29 {ECO:0000255|HAMAP-Rule:MF_00083, ECO:0000269|PubMed:11812233, ECO:0000269|PubMed:12069408};
GN   Name=pth {ECO:0000255|HAMAP-Rule:MF_00083};
OS   Staphylococcus aureus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND CIRCULAR DICHROISM ANALYSIS.
RC   STRAIN=ISP3 {ECO:0000269|PubMed:11812233};
RX   PubMed=11812233; DOI=10.1006/prep.2001.1540;
RA   Bonin P.D., Choi G.H., Trepod C.M., Mott J.E., Lyle S.B., Cialdella J.I.,
RA   Sarver R.W., Marshall V.P., Erickson L.A.;
RT   "Expression, purification, and characterization of peptidyl-tRNA hydrolase
RT   from Staphylococcus aureus.";
RL   Protein Expr. Purif. 24:123-130(2002).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP   SPECIFICITY.
RX   PubMed=12069408; DOI=10.1006/abio.2002.5700;
RA   Bonin P.D., Erickson L.A.;
RT   "Development of a fluorescence polarization assay for peptidyl-tRNA
RT   hydrolase.";
RL   Anal. Biochem. 306:8-16(2002).
CC   -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs
CC       which drop off the ribosome during protein synthesis. Hydrolyzes
CC       peptidyl-tRNAs and N-blocked aminoacyl-tRNAs but does not hydrolyze
CC       unblocked aminoacyl-tRNAs in vitro. {ECO:0000269|PubMed:12069408}.
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         ECO:0000269|PubMed:11812233, ECO:0000269|PubMed:12069408};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.8 uM for diacetyl-[(3)H]-Lys-tRNA(Lys)
CC         {ECO:0000269|PubMed:11812233};
CC         KM=127 nM for boron-dipyrromethene (BODIPY) labeled Lys-tRNA(Lys)
CC         {ECO:0000269|PubMed:12069408};
CC       pH dependence:
CC         Optimum pH is 7.0. {ECO:0000269|PubMed:11812233};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00083}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the PTH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00083}.
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DR   EMBL; AY035553; AAK61416.1; -; Genomic_DNA.
DR   RefSeq; WP_000649791.1; NZ_WYDB01000010.1.
DR   AlphaFoldDB; Q6YP15; -.
DR   SMR; Q6YP15; -.
DR   OMA; HVLSKFH; -.
DR   BRENDA; 3.1.1.29; 3352.
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   Cytoplasm; Hydrolase.
FT   CHAIN           1..190
FT                   /note="Peptidyl-tRNA hydrolase"
FT                   /id="PRO_0000187819"
SQ   SEQUENCE   190 AA;  21703 MW;  1F5E8C2502C466D8 CRC64;
     MKCIVGLGNI GKRFELTRHN IGFEVVDYIL EKNNFSLDKQ KFKGAYTIER MNGDKVLFIE
     PMTMMNLSGE AVAPIMDYYN VNPEDLIVLY DDLDLEQGQV RLRQKGSAGG HNGMKSIIKM
     LGTDQFKRIR IGVGRPTNGM TVPDYVLQRF SNDEMVTMEK VIEHAARAIE KFVETSRFDH
     VMNEFNGEVK