AC   MF_00083;
DC   Protein; auto
TR   HAMAP; MF_00083; -; 1; level=0
XX
Names: Pept_tRNA_hydro_bact
XX
ID   PTH
DE   RecName: Full=Peptidyl-tRNA hydrolase;
DE            Short=Pth;
DE            EC=3.1.1.29;
GN   Name=pth;
XX
CC   -!- FUNCTION: Hydrolyzes ribosome-free peptidyl-tRNAs (with 1 or more amino
CC       acids incorporated), which drop off the ribosome during protein
CC       synthesis, or as a result of ribosome stalling.
CC   -!- FUNCTION: Catalyzes the release of premature peptidyl moieties from
CC       peptidyl-tRNA molecules trapped in stalled 50S ribosomal subunits, and
CC       thus maintains levels of free tRNAs and 50S ribosomes.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acyl-L-alpha-aminoacyl-tRNA + H2O = an N-acyl-L-amino
CC         acid + a tRNA + 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;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the PTH family.
XX
DR   Pfam; PF01195; Pept_tRNA_hydro; 1; trigger=no
DR   NCBIfam; TIGR00447; Pth; 1; trigger=no
DR   PROSITE; PS01195; PEPT_TRNA_HYDROL_1; 1; trigger=no
DR   PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1; trigger=no
XX
KW   Cytoplasm
KW   Hydrolase
KW   RNA-binding
KW   tRNA-binding
XX
GO   GO:0004045; F:peptidyl-tRNA hydrolase activity
GO   GO:0005737; C:cytoplasm
GO   GO:0000049; F:tRNA binding
GO   GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins
GO   GO:0072344; P:rescue of stalled ribosome
XX
FT   From: PTH_ECOLI (P0A7D1)
FT   ACT_SITE        21
FT                   /note="Proton acceptor"
FT   Condition: H
FT   BINDING         16
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT   Condition: [YFH]
FT   BINDING         67
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT   Condition: [FYM]
FT   BINDING         69
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT   Optional; Condition: N
FT   BINDING         115
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT   Optional; Condition: N
FT   SITE            11
FT                   /note="Discriminates between blocked and unblocked aminoacyl-tRNA"
FT   Condition: N
FT   SITE            94
FT                   /note="Stabilizes the basic form of H active site to accept a proton"
FT   Condition: D
XX
Size: 172-250;
Related: None;
Template: P0A7D1; P37470; Q6YP15; Q9HVC3;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: in CORGL, CORJK
Plasmid: None
Comments: Originally called spoVC in BACSU. Reviewed in 2024, see PubMedID 38927071.
XX
# Version: 20
# Last updated date: 2025-03-21
# Created date: 2005-02-28
//