PTH_CAMJR
ID PTH_CAMJR Reviewed; 181 AA.
AC Q5HWF9;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=CJE0357;
OS Campylobacter jejuni (strain RM1221).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=195099;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM1221;
RX PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
RA Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
RA Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
RA Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
RA Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
RA Nelson K.E.;
RT "Major structural differences and novel potential virulence mechanisms from
RT the genomes of multiple Campylobacter species.";
RL PLoS Biol. 3:72-85(2005).
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 -!- 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; CP000025; AAW34946.1; -; Genomic_DNA.
DR RefSeq; WP_002854409.1; NC_003912.7.
DR AlphaFoldDB; Q5HWF9; -.
DR SMR; Q5HWF9; -.
DR KEGG; cjr:CJE0357; -.
DR HOGENOM; CLU_062456_4_1_7; -.
DR OMA; HVLSKFH; -.
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 3: Inferred from homology;
KW Cytoplasm; Hydrolase.
FT CHAIN 1..181
FT /note="Peptidyl-tRNA hydrolase"
FT /id="PRO_0000187713"
SQ SEQUENCE 181 AA; 19961 MW; D978D00710A7DEDF CRC64;
MILVVGLGNI GVEYENTRHN VGFMLIDLLL KESNFTNLTN SKFKGELFKI GSSLLLLKPS
TYMNNSGLSV KAVNDFYKCE RMIVIHDDID INLGALRFKK GGSSGGHNGL KSIDTLCGND
YERVRIGVGK GENVISHVLG KFKPEEEITL SKVLEHTKKA LLELIENDDL SAISSKYSLK
A