PTH_MYCTU
ID PTH_MYCTU Reviewed; 191 AA.
AC P9WHN7; L0T723; P65865; P96386;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 38.
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=Rv1014c;
GN ORFNames=MTCY10G2.35;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; AL123456; CCP43764.1; -; Genomic_DNA.
DR PIR; A70622; A70622.
DR RefSeq; NP_215530.1; NC_000962.3.
DR RefSeq; WP_003405251.1; NZ_NVQJ01000018.1.
DR PDB; 2JRC; NMR; -; A=1-191.
DR PDB; 2Z2I; X-ray; 1.98 A; A=1-191.
DR PDB; 2Z2J; X-ray; 2.35 A; A/B=1-191.
DR PDB; 2Z2K; X-ray; 2.50 A; A=1-191.
DR PDB; 3TCK; X-ray; 2.30 A; A=1-191.
DR PDB; 3TCN; X-ray; 2.30 A; A/B=1-191.
DR PDB; 3TD2; X-ray; 2.50 A; A=1-191.
DR PDB; 3TD6; X-ray; 3.20 A; A=1-191.
DR PDB; 7WT6; X-ray; 1.94 A; A=1-191.
DR PDBsum; 2JRC; -.
DR PDBsum; 2Z2I; -.
DR PDBsum; 2Z2J; -.
DR PDBsum; 2Z2K; -.
DR PDBsum; 3TCK; -.
DR PDBsum; 3TCN; -.
DR PDBsum; 3TD2; -.
DR PDBsum; 3TD6; -.
DR PDBsum; 7WT6; -.
DR AlphaFoldDB; P9WHN7; -.
DR SMR; P9WHN7; -.
DR STRING; 83332.Rv1014c; -.
DR PaxDb; P9WHN7; -.
DR DNASU; 886037; -.
DR GeneID; 45424985; -.
DR GeneID; 886037; -.
DR KEGG; mtu:Rv1014c; -.
DR TubercuList; Rv1014c; -.
DR eggNOG; COG0193; Bacteria.
DR OMA; HVLSKFH; -.
DR PhylomeDB; P9WHN7; -.
DR BRENDA; 3.1.1.29; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IDA:MTBBASE.
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_0000187780"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:2Z2I"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:2Z2I"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:2Z2I"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:2Z2I"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2JRC"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:2Z2I"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:2Z2I"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:2Z2I"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:2Z2I"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:2Z2I"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:2Z2I"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:2Z2I"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:2Z2I"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:2Z2I"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:2Z2I"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:2JRC"
FT HELIX 146..150
FT /evidence="ECO:0007829|PDB:2Z2I"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:2Z2I"
FT HELIX 162..178
FT /evidence="ECO:0007829|PDB:2Z2I"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:3TD2"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:3TCN"
SQ SEQUENCE 191 AA; 20456 MW; 1826278CBBA170BD CRC64;
MAEPLLVVGL GNPGANYART RHNLGFVVAD LLAARLGAKF KAHKRSGAEV ATGRSAGRSL
VLAKPRCYMN ESGRQIGPLA KFYSVAPANI IVIHDDLDLE FGRIRLKIGG GEGGHNGLRS
VVAALGTKDF QRVRIGIGRP PGRKDPAAFV LENFTPAERA EVPTICEQAA DATELLIEQG
MEPAQNRVHA W
