PTH_PSEAE
ID PTH_PSEAE Reviewed; 194 AA.
AC Q9HVC3;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=PA4672;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG08059.1; -; Genomic_DNA.
DR PIR; H83060; H83060.
DR RefSeq; NP_253361.1; NC_002516.2.
DR RefSeq; WP_003099278.1; NZ_QZGE01000029.1.
DR PDB; 4DHW; X-ray; 2.43 A; A/B=1-194.
DR PDB; 4DJJ; X-ray; 2.94 A; A/B=1-194.
DR PDB; 4ERX; X-ray; 2.50 A; A/B=1-194.
DR PDB; 4FNO; X-ray; 2.25 A; A/B=1-194.
DR PDB; 4FYJ; X-ray; 1.77 A; A=2-193.
DR PDB; 4JC4; X-ray; 2.25 A; A=1-194.
DR PDB; 4QAJ; X-ray; 1.50 A; A=1-194.
DR PDB; 4QBK; X-ray; 1.77 A; A=1-194.
DR PDB; 4QD3; X-ray; 1.89 A; A=1-194.
DR PDBsum; 4DHW; -.
DR PDBsum; 4DJJ; -.
DR PDBsum; 4ERX; -.
DR PDBsum; 4FNO; -.
DR PDBsum; 4FYJ; -.
DR PDBsum; 4JC4; -.
DR PDBsum; 4QAJ; -.
DR PDBsum; 4QBK; -.
DR PDBsum; 4QD3; -.
DR AlphaFoldDB; Q9HVC3; -.
DR SMR; Q9HVC3; -.
DR STRING; 287.DR97_1982; -.
DR PaxDb; Q9HVC3; -.
DR PRIDE; Q9HVC3; -.
DR EnsemblBacteria; AAG08059; AAG08059; PA4672.
DR GeneID; 881396; -.
DR KEGG; pae:PA4672; -.
DR PATRIC; fig|208964.12.peg.4894; -.
DR PseudoCAP; PA4672; -.
DR HOGENOM; CLU_062456_3_1_6; -.
DR InParanoid; Q9HVC3; -.
DR OMA; HVLSKFH; -.
DR PhylomeDB; Q9HVC3; -.
DR BioCyc; PAER208964:G1FZ6-4769-MON; -.
DR BRENDA; 3.1.1.29; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IBA:GO_Central.
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; Hydrolase; Reference proteome.
FT CHAIN 1..194
FT /note="Peptidyl-tRNA hydrolase"
FT /id="PRO_0000187796"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:4QAJ"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:4QAJ"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:4QAJ"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:4QAJ"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:4QAJ"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:4QAJ"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:4QAJ"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:4QAJ"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:4QAJ"
FT HELIX 72..83
FT /evidence="ECO:0007829|PDB:4QAJ"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:4QAJ"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:4QAJ"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:4QAJ"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:4QAJ"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:4FYJ"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:4QAJ"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:4QAJ"
FT HELIX 147..151
FT /evidence="ECO:0007829|PDB:4QAJ"
FT HELIX 157..172
FT /evidence="ECO:0007829|PDB:4QAJ"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:4QAJ"
FT HELIX 182..190
FT /evidence="ECO:0007829|PDB:4QAJ"
SQ SEQUENCE 194 AA; 20804 MW; A6E14ECBF84B61AA CRC64;
MTAVQLIVGL GNPGPEYDQT RHNAGALFVE RLAHAQGVSL VADRKYFGLV GKFSHQGKDV
RLLIPTTYMN RSGQSVAALA GFFRIAPDAI LVAHDELDMP PGVAKLKTGG GHGGHNGLRD
IIAQLGNQNS FHRLRLGIGH PGHSSLVSGY VLGRAPRSEQ ELLDTSIDFA LGVLPEMLAG
DWTRAMQKLH SQKA
