ID   PTH_ANADE               Reviewed;         192 AA.
AC   Q2IM62;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   04-NOV-2026, entry version 99.
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=Adeh_0119;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Pseudomonadati; Myxococcota; Myxococcia; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA   Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA   Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00083}.
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       {ECO:0000255|HAMAP-Rule:MF_00083}.
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; 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; CP000251; ABC79896.1; -; Genomic_DNA.
DR   RefSeq; WP_011419179.1; NC_007760.1.
DR   AlphaFoldDB; Q2IM62; -.
DR   SMR; Q2IM62; -.
DR   STRING; 290397.Adeh_0119; -.
DR   KEGG; ade:Adeh_0119; -.
DR   eggNOG; COG0193; Bacteria.
DR   HOGENOM; CLU_062456_2_2_7; -.
DR   OMA; AACWLFE; -.
DR   OrthoDB; 9800507at2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004045; F:peptidyl-tRNA hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR   GO; GO:0072344; P:rescue of stalled cytosolic ribosome; IEA:UniProtKB-UniRule.
DR   CDD; cd00462; PTH; 1.
DR   FunFam; 3.40.50.1470:FF:000001; Peptidyl-tRNA hydrolase; 1.
DR   Gene3D; 3.40.50.1470; Peptidyl-tRNA hydrolase; 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   NCBIfam; TIGR00447; pth; 1.
DR   PANTHER; PTHR17224; PEPTIDYL-TRNA HYDROLASE; 1.
DR   PANTHER; PTHR17224:SF1; PEPTIDYL-TRNA HYDROLASE; 1.
DR   Pfam; PF01195; Pept_tRNA_hydro; 1.
DR   SUPFAM; SSF53178; Peptidyl-tRNA hydrolase-like; 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; RNA-binding; tRNA-binding.
FT   CHAIN           1..192
FT                   /note="Peptidyl-tRNA hydrolase"
FT                   /id="PRO_0000264003"
FT   ACT_SITE        19
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00083"
FT   BINDING         14
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00083"
FT   BINDING         64
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00083"
FT   BINDING         66
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00083"
FT   BINDING         112
FT                   /ligand="tRNA"
FT                   /ligand_id="ChEBI:CHEBI:17843"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00083"
FT   SITE            9
FT                   /note="Discriminates between blocked and unblocked
FT                   aminoacyl-tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00083"
FT   SITE            91
FT                   /note="Stabilizes the basic form of H active site to accept
FT                   a proton"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00083"
SQ   SEQUENCE   192 AA;  20717 MW;  442847C4A5D3024E CRC64;
     MKLVVGLGNP GEEYARTRHN VGFVVADRLA QLAGASFTAK KFAAELAEAR LGPERVWILK
     PQTYMNHSGE AVGAALRFWK LGLDDLVVVH DDLELEPFRV QLKVGGGHGG HNGVKSVNAH
     VGSPEYARVR VGVGRPPPRM DPADYVLGKF AKGEDAELDL CVEQAVEATR LAVELGAAKA
     MNQVNRRSRA AE
//