PTH_MYCS2
ID PTH_MYCS2 Reviewed; 191 AA.
AC A0R3D3; I7FK76;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 99.
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=MSMEG_5432, MSMEI_5283;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
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; CP000480; ABK75581.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP41725.1; -; Genomic_DNA.
DR RefSeq; WP_011730530.1; NZ_SIJM01000006.1.
DR RefSeq; YP_889671.1; NC_008596.1.
DR PDB; 2LGJ; NMR; -; A=1-191.
DR PDB; 2NAF; NMR; -; A=1-191.
DR PDB; 3KJZ; X-ray; 2.40 A; A=1-191.
DR PDB; 3KK0; X-ray; 2.65 A; A=1-191.
DR PDB; 3P2J; X-ray; 2.22 A; A=1-191.
DR PDBsum; 2LGJ; -.
DR PDBsum; 2NAF; -.
DR PDBsum; 3KJZ; -.
DR PDBsum; 3KK0; -.
DR PDBsum; 3P2J; -.
DR AlphaFoldDB; A0R3D3; -.
DR BMRB; A0R3D3; -.
DR SMR; A0R3D3; -.
DR STRING; 246196.MSMEI_5283; -.
DR EnsemblBacteria; ABK75581; ABK75581; MSMEG_5432.
DR EnsemblBacteria; AFP41725; AFP41725; MSMEI_5283.
DR GeneID; 66736735; -.
DR KEGG; msg:MSMEI_5283; -.
DR KEGG; msm:MSMEG_5432; -.
DR PATRIC; fig|246196.19.peg.5293; -.
DR eggNOG; COG0193; Bacteria.
DR OMA; HVLSKFH; -.
DR OrthoDB; 1676462at2; -.
DR BRENDA; 3.1.1.29; 3512.
DR EvolutionaryTrace; A0R3D3; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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; -; 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..191
FT /note="Peptidyl-tRNA hydrolase"
FT /id="PRO_1000010613"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:3P2J"
FT TURN 15..19
FT /evidence="ECO:0007829|PDB:3P2J"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:3P2J"
FT HELIX 24..36
FT /evidence="ECO:0007829|PDB:3P2J"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2LGJ"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:3P2J"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:3P2J"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:3P2J"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:2NAF"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:3P2J"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:3P2J"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:3P2J"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:3P2J"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:3P2J"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:3P2J"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:3P2J"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3KK0"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:3P2J"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:3P2J"
FT HELIX 162..179
FT /evidence="ECO:0007829|PDB:3P2J"
FT HELIX 181..188
FT /evidence="ECO:0007829|PDB:3P2J"
SQ SEQUENCE 191 AA; 20278 MW; BA77A2644BDD6419 CRC64;
MAEPLLVVGL GNPGPTYAKT RHNLGFMVAD VLAGRIGSAF KVHKKSGAEV VTGRLAGTSV
VLAKPRCYMN ESGRQVGPLA KFYSVPPQQI VVIHDELDID FGRIRLKLGG GEGGHNGLRS
VASALGTKNF HRVRIGVGRP PGRKDPAAFV LENFTAAERA EVPTIVEQAA DATELLIAQG
LEPAQNTVHA W
