ID PTH_SALTI Reviewed; 194 AA.
AC P0A282; Q60001;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 104.
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=STY1909, t1093;
OS Salmonella typhi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IMSS-1;
RX PubMed=8635758; DOI=10.1016/0378-1119(95)00823-3;
RA de la Vega F.M., Galindo J.M., Old I.G., Guarneros G.;
RT "Microbial genes homologous to the peptidyl-tRNA hydrolase-encoding gene of
RT Escherichia coli.";
RL Gene 169:97-100(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs
CC which drop off the ribosome during protein synthesis. Involved in
CC lambda inhibition of host protein synthesis. PTH activity may, directly
CC or indirectly, be the target for lambda bar RNA leading to rap cell
CC death.
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.
CC -!- SIMILARITY: Belongs to the PTH family. {ECO:0000255|HAMAP-
CC Rule:MF_00083}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO68756.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD02138.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U31571; AAB06185.1; -; Genomic_DNA.
DR EMBL; AL513382; CAD02138.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE014613; AAO68756.1; ALT_INIT; Genomic_DNA.
DR PIR; AI0720; AI0720.
DR RefSeq; NP_456293.1; NC_003198.1.
DR RefSeq; WP_000985595.1; NZ_WSUN01000006.1.
DR AlphaFoldDB; P0A282; -.
DR SMR; P0A282; -.
DR STRING; 220341.gene:17585832; -.
DR KEGG; stt:t1093; -.
DR KEGG; sty:STY1909; -.
DR PATRIC; fig|220341.7.peg.1924; -.
DR eggNOG; COG0193; Bacteria.
DR HOGENOM; CLU_062456_3_1_6; -.
DR OMA; PNTYMNL; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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; 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-RELATED; 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; Hydrolase.
FT CHAIN 1..194
FT /note="Peptidyl-tRNA hydrolase"
FT /id="PRO_0000187809"
FT CONFLICT 33..34
FT /note="ER -> DG (in Ref. 1; AAB06185)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 194 AA; 21178 MW; 9D6AC85C59B92831 CRC64;
MAIKLIVGLA NPGAEYAATR HNAGAWYVDL LAERLRAPLR EEPKFFGYTS RITLEGEDVR
LLVPTTFMNL SGKAVGAMAS FYRIQPDEIL VAHDELDLPP GVAKFKLGGG HGGHNGLKDI
ISKLGNNPNF HRLRVGIGHP GDKNKVVGFV LGKPPVSEQK LIDEAIDEAA RCTELWFKEG
LAKATSRLHT FKAQ
//
