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Database: UniProt
Entry: A4VS92
LinkDB: A4VS92
Original site: A4VS92 
ID   PTH_STRSY               Reviewed;         189 AA.
AC   A4VS92;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   01-OCT-2014, entry version 49.
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};
GN   OrderedLocusNames=SSU05_0007;
OS   Streptococcus suis (strain 05ZYH33).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=391295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05ZYH33;
RX   PubMed=17375201; DOI=10.1371/journal.pone.0000315;
RA   Chen C., Tang J., Dong W., Wang C., Feng Y., Wang J., Zheng F.,
RA   Pan X., Liu D., Li M., Song Y., Zhu X., Sun H., Feng T., Guo Z.,
RA   Ju A., Ge J., Dong Y., Sun W., Jiang Y., Wang J., Yan J., Yang H.,
RA   Wang X., Gao G.F., Yang R., Wang J., Yu J.;
RT   "A glimpse of streptococcal toxic shock syndrome from comparative
RT   genomics of S. suis 2 Chinese isolates.";
RL   PLoS ONE 2:E315-E315(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; CP000407; ABP88981.1; -; Genomic_DNA.
DR   RefSeq; YP_001197381.1; NC_009442.1.
DR   ProteinModelPortal; A4VS92; -.
DR   STRING; 391295.SSU05_0007; -.
DR   EnsemblBacteria; ABP88981; ABP88981; SSU05_0007.
DR   GeneID; 5099249; -.
DR   KEGG; ssu:SSU05_0007; -.
DR   PATRIC; 19771682; VBIStrSui128929_0007.
DR   eggNOG; COG0193; -.
DR   HOGENOM; HOG000004797; -.
DR   KO; K01056; -.
DR   OMA; MGVVEHV; -.
DR   OrthoDB; EOG6C5RTR; -.
DR   BioCyc; SSUI391295:GHI8-75-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; Reference proteome.
FT   CHAIN         1    189       Peptidyl-tRNA hydrolase.
FT                                /FTId=PRO_1000010659.
SQ   SEQUENCE   189 AA;  21259 MW;  DE76D51BE063B15C CRC64;
     MTRLIIGLGN PGDRYFETKH NVGFMLLDKI AKRENVTFNH DKIFQADIAT TFIDGEKIYL
     VKPTTFMNES GKAVHALMTY YGLDATDILV AYDDLDMAVG KIRFRQKGSA GGHNGIKSIV
     KHIGTQEFDR IKIGIGRPKG KMSVVNHVLS GFDIEDRIEI DLALDKLDKA VNVYLEEDDF
     DTVMRKFNG
//
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