ID   PTH_CAMJE               Reviewed;         181 AA.
AC   Q9PII7; Q0PBJ7;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   10-JUN-2026, entry version 122.
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}; OrderedLocusNames=Cj0312;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 /
OS   NCTC 11168).
OC   Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria;
OC   Campylobacterales; Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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; AL111168; CAL34463.1; -; Genomic_DNA.
DR   PIR; D81450; D81450.
DR   RefSeq; WP_002858659.1; NC_002163.1.
DR   RefSeq; YP_002343750.1; NC_002163.1.
DR   AlphaFoldDB; Q9PII7; -.
DR   SMR; Q9PII7; -.
DR   IntAct; Q9PII7; 1.
DR   STRING; 192222.Cj0312; -.
DR   PaxDb; 192222-Cj0312; -.
DR   EnsemblBacteria; CAL34463; CAL34463; Cj0312.
DR   GeneID; 904636; -.
DR   KEGG; cje:Cj0312; -.
DR   PATRIC; fig|192222.6.peg.304; -.
DR   eggNOG; COG0193; Bacteria.
DR   HOGENOM; CLU_062456_4_1_7; -.
DR   OrthoDB; 9800507at2; -.
DR   Proteomes; UP000000799; Chromosome.
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; Reference proteome; RNA-binding; tRNA-binding.
FT   CHAIN           1..181
FT                   /note="Peptidyl-tRNA hydrolase"
FT                   /id="PRO_0000187712"
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         62
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         108
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            87
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   181 AA;  19921 MW;  6229950710A523F0 CRC64;
     MILVVGLGNI GVEYENTRHN VGFMLIDLLL KESNFTNLTN SKFKGELFKI GSSLLLLKPS
     TYMNNSGLSV KAVNDFYKCE RMIVIHDDID INLGALRFKK GGSSGGHNGL KSIDTLCGND
     YERVRIGVGK GENVISHVLG KFKSEEEITL SKVLEHAKKA LLELIENDDL SAISSKYSLK
     A
//