ID B9KDP0_CAMLR Unreviewed; 179 AA. AC B9KDP0; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 2. DT 10-JUN-2026, entry version 72. DE RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000256|ARBA:ARBA00050038, ECO:0000256|HAMAP-Rule:MF_00083}; DE Short=Pth {ECO:0000256|HAMAP-Rule:MF_00083}; DE EC=3.1.1.29 {ECO:0000256|ARBA:ARBA00013260, ECO:0000256|HAMAP-Rule:MF_00083}; GN Name=pth {ECO:0000256|HAMAP-Rule:MF_00083, GN ECO:0000313|EMBL:ACM64678.2}; GN OrderedLocusNames=Cla_1363 {ECO:0000313|EMBL:ACM64678.2}; OS Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060). OC Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria; OC Campylobacterales; Campylobacteraceae; Campylobacter. OX NCBI_TaxID=306263 {ECO:0000313|EMBL:ACM64678.2, ECO:0000313|Proteomes:UP000007727}; RN [1] {ECO:0000313|EMBL:ACM64678.2, ECO:0000313|Proteomes:UP000007727} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RM2100 / D67 / ATCC BAA-1060 RC {ECO:0000313|Proteomes:UP000007727}; RX PubMed=18713059; DOI=10.1089/fpd.2008.0101; RA Miller W.G., Wang G., Binnewies T.T., Parker C.T.; RT "The complete genome sequence and analysis of the human pathogen RT Campylobacter lari."; RL Foodborne Pathog. Dis. 5:371-386(2008). 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:0000256|HAMAP-Rule:MF_00083}. 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:0000256|HAMAP- CC 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:0000256|HAMAP-Rule:MF_00083, CC ECO:0000256|RuleBase:RU000673}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00083}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00083}. CC -!- SIMILARITY: Belongs to the PTH family. {ECO:0000256|ARBA:ARBA00038063, CC ECO:0000256|HAMAP-Rule:MF_00083, ECO:0000256|RuleBase:RU004320}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000932; ACM64678.2; -; Genomic_DNA. DR RefSeq; WP_012662062.1; NC_012039.1. DR AlphaFoldDB; B9KDP0; -. DR SMR; B9KDP0; -. DR KEGG; cla:CLA_1363; -. DR PATRIC; fig|306263.5.peg.1349; -. DR eggNOG; COG0795; Bacteria. DR HOGENOM; CLU_065978_0_0_7; -. DR Proteomes; UP000007727; 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 {ECO:0000256|HAMAP-Rule:MF_00083}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00083}; KW Reference proteome {ECO:0000313|Proteomes:UP000007727}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_00083}; KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP- KW Rule:MF_00083}. FT ACT_SITE 19 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00083" FT BINDING 14 FT /ligand="tRNA" FT /ligand_id="ChEBI:CHEBI:17843" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00083" FT BINDING 61 FT /ligand="tRNA" FT /ligand_id="ChEBI:CHEBI:17843" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00083" FT BINDING 63 FT /ligand="tRNA" FT /ligand_id="ChEBI:CHEBI:17843" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00083" FT BINDING 107 FT /ligand="tRNA" FT /ligand_id="ChEBI:CHEBI:17843" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00083" FT SITE 9 FT /note="Discriminates between blocked and unblocked FT aminoacyl-tRNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00083" FT SITE 86 FT /note="Stabilizes the basic form of H active site to accept FT a proton" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00083" SQ SEQUENCE 179 AA; 19886 MW; 1F70B5110DC6CB49 CRC64; MTLVVGLGNI GEQYAQTRHN VGFMLIDLLL KDLEVAKLSN TKFKGELFKS SLAFFLKPST YMNLSGESVK AVSDFYKCDR IIVIHDDIDL NLGTLKFKIG GSSGGHNGLK SIDNLCGNAY ERVRIGVGKD QDVISHVLGK FKQEEQESLN KVLEQAKKAL FELLKSNIEQ VASKYSIRN //