PTH_XANOP
ID PTH_XANOP Reviewed; 194 AA.
AC B2SQP2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=PXO_04540;
OS Xanthomonas oryzae pv. oryzae (strain PXO99A).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=360094;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PXO99A;
RX PubMed=18452608; DOI=10.1186/1471-2164-9-204;
RA Salzberg S.L., Sommer D.D., Schatz M.C., Phillippy A.M., Rabinowicz P.D.,
RA Tsuge S., Furutani A., Ochiai H., Delcher A.L., Kelley D., Madupu R.,
RA Puiu D., Radune D., Shumway M., Trapnell C., Aparna G., Jha G., Pandey A.,
RA Patil P.B., Ishihara H., Meyer D.F., Szurek B., Verdier V., Koebnik R.,
RA Dow J.M., Ryan R.P., Hirata H., Tsuyumu S., Won Lee S., Seo Y.-S.,
RA Sriariyanum M., Ronald P.C., Sonti R.V., Van Sluys M.-A., Leach J.E.,
RA White F.F., Bogdanove A.J.;
RT "Genome sequence and rapid evolution of the rice pathogen Xanthomonas
RT oryzae pv. oryzae PXO99A.";
RL BMC Genomics 9:204-204(2008).
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; CP000967; ACD57869.1; -; Genomic_DNA.
DR RefSeq; WP_011260042.1; NC_010717.2.
DR AlphaFoldDB; B2SQP2; -.
DR SMR; B2SQP2; -.
DR STRING; 360094.PXO_04540; -.
DR EnsemblBacteria; ACD57869; ACD57869; PXO_04540.
DR KEGG; xop:PXO_04540; -.
DR eggNOG; COG0193; Bacteria.
DR HOGENOM; CLU_062456_3_1_6; -.
DR OMA; HVLSKFH; -.
DR OrthoDB; 1676462at2; -.
DR Proteomes; UP000001740; Chromosome.
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.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase.
FT CHAIN 1..194
FT /note="Peptidyl-tRNA hydrolase"
FT /id="PRO_1000093002"
SQ SEQUENCE 194 AA; 21038 MW; 867236C14DAB2D7C CRC64;
MSALRLIVGL GNPGQEHAQT RHNAGFRFVD SLIERSGARW ALDSKLFGET AKVDIAGQPV
WLLKPATFMN LSGKSITAAL RFWKIEPEHL LVAHDELDLA PGTARLKFDG GHGGQNGLRD
TIGLLGHGKF HRLRVGIGHP GHKDRVVPWV LGRAGREDDA AIGTAIDAAI DVLPLAMEGH
FSEAMKRLHT SRDA