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Database: UniProt
Entry: Q2YVY3
LinkDB: Q2YVY3
Original site: Q2YVY3 
ID   PTH_STAAB               Reviewed;         190 AA.
AC   Q2YVY3;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   29-OCT-2014, entry version 64.
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=SAB0451;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus
RT   aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
CC   -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-
CC       tRNAs which drop off the ribosome during protein synthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00083}.
CC   -!- CATALYTIC ACTIVITY: N-substituted aminoacyl-tRNA + H(2)O = N-
CC       substituted amino acid + tRNA. {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; AJ938182; CAI80139.1; -; Genomic_DNA.
DR   RefSeq; YP_415950.1; NC_007622.1.
DR   ProteinModelPortal; Q2YVY3; -.
DR   STRING; 273036.SAB0451; -.
DR   EnsemblBacteria; CAI80139; CAI80139; SAB0451.
DR   GeneID; 3793239; -.
DR   KEGG; sab:SAB0451; -.
DR   PATRIC; 19521651; VBIStaAur92441_0490.
DR   eggNOG; COG0193; -.
DR   HOGENOM; HOG000004797; -.
DR   KO; K01056; -.
DR   OMA; PGKEYEK; -.
DR   OrthoDB; EOG6C5RTR; -.
DR   BioCyc; SAUR273036:GJVS-457-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA:UniProtKB-EC.
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   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   Complete proteome; Cytoplasm; Hydrolase.
FT   CHAIN         1    190       Peptidyl-tRNA hydrolase.
FT                                /FTId=PRO_0000264112.
SQ   SEQUENCE   190 AA;  21689 MW;  193EEA2502C466D8 CRC64;
     MKCIVGLGNI GKRFELTRHN IGFEVVDYIL EKNNFSLDKQ KFKGAYTIER MNGDKVLFIE
     PMTMMNLSGE AVAPIMDYYN VNPEDLIVLY DDLDLEQGQV RLRQKGSAGG HNGMKSIIKM
     LGTDQFKRIR IGVGRPTNGM TVPDYVLQRF SNDEMVTMEK VIEHAGRAIE KFVETSRFDH
     VMNEFNGEVK
//
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