PTH_VIBC3
ID PTH_VIBC3 Reviewed; 196 AA.
AC A5F686; C3M3E1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 81.
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=VC0395_A1761, VC395_2298;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000627; ABQ21972.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP10290.1; -; Genomic_DNA.
DR RefSeq; WP_000081944.1; NZ_JAACZH010000001.1.
DR PDB; 5GVZ; X-ray; 1.75 A; A=2-196.
DR PDBsum; 5GVZ; -.
DR AlphaFoldDB; A5F686; -.
DR BMRB; A5F686; -.
DR SMR; A5F686; -.
DR STRING; 345073.VC395_2298; -.
DR EnsemblBacteria; ABQ21972; ABQ21972; VC0395_A1761.
DR KEGG; vco:VC0395_A1761; -.
DR KEGG; vcr:VC395_2298; -.
DR PATRIC; fig|345073.21.peg.2215; -.
DR eggNOG; COG0193; Bacteria.
DR HOGENOM; CLU_062456_3_1_6; -.
DR OMA; HVLSKFH; -.
DR Proteomes; UP000000249; Chromosome 2.
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.
FT CHAIN 1..196
FT /note="Peptidyl-tRNA hydrolase"
FT /id="PRO_1000071233"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:5GVZ"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:5GVZ"
FT HELIX 25..36
FT /evidence="ECO:0007829|PDB:5GVZ"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:5GVZ"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:5GVZ"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:5GVZ"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:5GVZ"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:5GVZ"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:5GVZ"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:5GVZ"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:5GVZ"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:5GVZ"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:5GVZ"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:5GVZ"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:5GVZ"
FT HELIX 148..152
FT /evidence="ECO:0007829|PDB:5GVZ"
FT HELIX 158..181
FT /evidence="ECO:0007829|PDB:5GVZ"
FT HELIX 183..190
FT /evidence="ECO:0007829|PDB:5GVZ"
SQ SEQUENCE 196 AA; 21483 MW; 6D5F7C3D6E4F6304 CRC64;
MSQPIKLLVG LANPGPEYAK TRHNAGAWVV EELARIHNVT LKNEPKFFGL TGRLLINSQE
LRVLIPTTFM NLSGKAIAAL ANFYQIKPEE IMVAHDELDL PPGVAKFKQG GGHGGHNGLK
DTISKLGNNK EFYRLRLGIG HPGHKDKVAG YVLGKAPAKE QECLDAAVDE SVRCLEILMK
DGLTKAQNRL HTFKAE
