PTH_ECOLI
ID PTH_ECOLI Reviewed; 194 AA.
AC P0A7D1; P23932;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 133.
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=b1204, JW1195;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-17.
RC STRAIN=K12;
RX PubMed=1833189; DOI=10.1002/j.1460-2075.1991.tb04919.x;
RA Garcia-Villegas M.R., de la Vega F.M., Galindo J.M., Segura M.,
RA Buckingham R.H., Guarneros G.;
RT "Peptidyl-tRNA hydrolase is involved in lambda inhibition of host protein
RT synthesis.";
RL EMBO J. 10:3549-3555(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP CRYSTALLIZATION.
RX PubMed=9144799;
RX DOI=10.1002/(sici)1097-0134(199705)28:1<135::aid-prot14>3.0.co;2-k;
RA Schmitt E., Fromant M., Plateau P., Mechulam Y., Blanquet S.;
RT "Crystallization and preliminary X-ray analysis of Escherichia coli
RT peptidyl-tRNA hydrolase.";
RL Proteins 28:135-136(1997).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).
RX PubMed=9303320; DOI=10.1093/emboj/16.15.4760;
RA Schmitt E., Mechulam Y., Fromant M., Plateau P., Blanquet S.;
RT "Crystal structure at 1.2-A resolution and active site mapping of
RT Escherichia coli peptidyl-tRNA hydrolase.";
RL EMBO J. 16:4760-4769(1997).
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the PTH family. {ECO:0000255|HAMAP-
CC Rule:MF_00083}.
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DR EMBL; X61941; CAA43945.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74288.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36062.1; -; Genomic_DNA.
DR PIR; S16753; S16753.
DR RefSeq; NP_415722.1; NC_000913.3.
DR RefSeq; WP_000152933.1; NZ_STEB01000023.1.
DR PDB; 2PTH; X-ray; 1.20 A; A=2-194.
DR PDB; 3VJR; X-ray; 2.40 A; A/C=1-194.
DR PDBsum; 2PTH; -.
DR PDBsum; 3VJR; -.
DR AlphaFoldDB; P0A7D1; -.
DR SMR; P0A7D1; -.
DR BioGRID; 4262870; 54.
DR DIP; DIP-35932N; -.
DR IntAct; P0A7D1; 16.
DR STRING; 511145.b1204; -.
DR jPOST; P0A7D1; -.
DR PaxDb; P0A7D1; -.
DR PRIDE; P0A7D1; -.
DR EnsemblBacteria; AAC74288; AAC74288; b1204.
DR EnsemblBacteria; BAA36062; BAA36062; BAA36062.
DR GeneID; 945765; -.
DR KEGG; ecj:JW1195; -.
DR KEGG; eco:b1204; -.
DR PATRIC; fig|1411691.4.peg.1080; -.
DR EchoBASE; EB0778; -.
DR eggNOG; COG0193; Bacteria.
DR HOGENOM; CLU_062456_3_1_6; -.
DR InParanoid; P0A7D1; -.
DR OMA; HVLSKFH; -.
DR PhylomeDB; P0A7D1; -.
DR BioCyc; EcoCyc:EG10785-MON; -.
DR BioCyc; MetaCyc:EG10785-MON; -.
DR BRENDA; 3.1.1.29; 2026.
DR SABIO-RK; P0A7D1; -.
DR EvolutionaryTrace; P0A7D1; -.
DR PRO; PR:P0A7D1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IDA:EcoCyc.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Reference proteome.
FT CHAIN 1..194
FT /note="Peptidyl-tRNA hydrolase"
FT /id="PRO_0000187733"
FT MUTAGEN 101
FT /note="G->D: Pth(ts) mutants synthesize thermosensitive PTH
FT and die at 42 degrees Celsius from a defect in protein
FT synthesis."
FT MUTAGEN 134
FT /note="R->H: Rap mutants do not support vegetative growth
FT of bacteriophage lambda and die upon transcription of
FT lambda DNA bar sites."
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:2PTH"
FT TURN 14..18
FT /evidence="ECO:0007829|PDB:2PTH"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:2PTH"
FT HELIX 23..35
FT /evidence="ECO:0007829|PDB:2PTH"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:2PTH"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:2PTH"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:2PTH"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:2PTH"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:2PTH"
FT HELIX 72..82
FT /evidence="ECO:0007829|PDB:2PTH"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:2PTH"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:2PTH"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:2PTH"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:2PTH"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:2PTH"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:2PTH"
FT HELIX 156..179
FT /evidence="ECO:0007829|PDB:2PTH"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:2PTH"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:2PTH"
SQ SEQUENCE 194 AA; 21082 MW; A28A69A63F2DD530 CRC64;
MTIKLIVGLA NPGAEYAATR HNAGAWFVDL LAERLRAPLR EEAKFFGYTS RVTLGGEDVR
LLVPTTFMNL SGKAVAAMAS FFRINPDEIL VAHDELDLPP GVAKFKLGGG HGGHNGLKDI
ISKLGNNPNF HRLRIGIGHP GDKNKVVGFV LGKPPVSEQK LIDEAIDEAA RCTEMWFTDG
LTKATNRLHA FKAQ
