ID   PTH_STRPZ               Reviewed;         189 AA.
AC   B5XIP6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000255|HAMAP-Rule:MF_00083, ECO:0000303|PubMed:25389518};
DE            Short=PTH {ECO:0000255|HAMAP-Rule:MF_00083, ECO:0000303|PubMed:25389518};
DE            EC=3.1.1.29 {ECO:0000255|HAMAP-Rule:MF_00083};
DE   AltName: Full=SpPth {ECO:0000303|PubMed:25389518};
GN   Name=pth {ECO:0000255|HAMAP-Rule:MF_00083}; OrderedLocusNames=Spy49_0005;
OS   Streptococcus pyogenes serotype M49 (strain NZ131).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=471876;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NZ131;
RX   PubMed=18820018; DOI=10.1128/jb.00672-08;
RA   McShan W.M., Ferretti J.J., Karasawa T., Suvorov A.N., Lin S., Qin B.,
RA   Jia H., Kenton S., Najar F., Wu H., Scott J., Roe B.A., Savic D.J.;
RT   "Genome sequence of a nephritogenic and highly transformable M49 strain of
RT   Streptococcus pyogenes.";
RL   J. Bacteriol. 190:7773-7785(2008).
RN   [2] {ECO:0007744|PDB:4QT4}
RP   X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS), AND SUBUNIT.
RX   PubMed=25389518; DOI=10.1016/j.fob.2014.10.010;
RA   Singh A., Gautam L., Sinha M., Bhushan A., Kaur P., Sharma S., Singh T.P.;
RT   "Crystal structure of peptidyl-tRNA hydrolase from a Gram-positive
RT   bacterium, Streptococcus pyogenes at 2.19 A resolution shows the closed
RT   structure of the substrate-binding cleft.";
RL   FEBS Open Bio 4:915-922(2014).
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       ECO:0000269|PubMed:25389518}.
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; CP000829; ACI60369.1; -; Genomic_DNA.
DR   RefSeq; WP_002981924.1; NC_011375.1.
DR   PDB; 4QT4; X-ray; 2.19 A; A/B=1-189.
DR   PDBsum; 4QT4; -.
DR   AlphaFoldDB; B5XIP6; -.
DR   SMR; B5XIP6; -.
DR   EnsemblBacteria; ACI60369; ACI60369; Spy49_0005.
DR   KEGG; soz:Spy49_0005; -.
DR   HOGENOM; CLU_062456_4_1_9; -.
DR   OMA; HVLSKFH; -.
DR   Proteomes; UP000001039; 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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Hydrolase.
FT   CHAIN           1..189
FT                   /note="Peptidyl-tRNA hydrolase"
FT                   /id="PRO_1000092994"
FT   STRAND          2..7
FT                   /evidence="ECO:0007829|PDB:4QT4"
FT   HELIX           13..15
FT                   /evidence="ECO:0007829|PDB:4QT4"
FT   HELIX           19..21
FT                   /evidence="ECO:0007829|PDB:4QT4"
FT   HELIX           22..33
FT                   /evidence="ECO:0007829|PDB:4QT4"
FT   STRAND          42..53
FT                   /evidence="ECO:0007829|PDB:4QT4"
FT   STRAND          56..63
FT                   /evidence="ECO:0007829|PDB:4QT4"
FT   HELIX           67..69
FT                   /evidence="ECO:0007829|PDB:4QT4"
FT   HELIX           70..80
FT                   /evidence="ECO:0007829|PDB:4QT4"
FT   HELIX           85..87
FT                   /evidence="ECO:0007829|PDB:4QT4"
FT   STRAND          88..97
FT                   /evidence="ECO:0007829|PDB:4QT4"
FT   STRAND          102..106
FT                   /evidence="ECO:0007829|PDB:4QT4"
FT   HELIX           114..123
FT                   /evidence="ECO:0007829|PDB:4QT4"
FT   STRAND          128..134
FT                   /evidence="ECO:0007829|PDB:4QT4"
FT   HELIX           144..148
FT                   /evidence="ECO:0007829|PDB:4QT4"
FT   HELIX           154..156
FT                   /evidence="ECO:0007829|PDB:4QT4"
FT   HELIX           157..177
FT                   /evidence="ECO:0007829|PDB:4QT4"
FT   HELIX           180..187
FT                   /evidence="ECO:0007829|PDB:4QT4"
SQ   SEQUENCE   189 AA;  21197 MW;  692D824497B1C01B CRC64;
     MVKMIVGLGN PGSKYEKTKH NIGFMAIDNI VKNLDVTFTD DKNFKAQIGS TFINHEKVYF
     VKPTTFMNNS GIAVKALLTY YNIDITDLIV IYDDLDMEVS KLRLRSKGSA GGHNGIKSII
     AHIGTQEFNR IKVGIGRPLK GMTVINHVMG QFNTEDNIAI SLTLDRVVNA VKFYLQENDF
     EKTMQKFNG