ID   PTH_VIBCM               Reviewed;         196 AA.
AC   C3LPI9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 65.
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=VCM66_2107;
OS   Vibrio cholerae serotype O1 (strain M66-2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=579112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M66-2;
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; CP001233; ACP06409.1; -; Genomic_DNA.
DR   RefSeq; WP_000081944.1; NC_012578.1.
DR   PDB; 2MJL; NMR; -; A=2-196.
DR   PDBsum; 2MJL; -.
DR   AlphaFoldDB; C3LPI9; -.
DR   BMRB; C3LPI9; -.
DR   SMR; C3LPI9; -.
DR   EnsemblBacteria; ACP06409; ACP06409; VCM66_2107.
DR   KEGG; vcm:VCM66_2107; -.
DR   HOGENOM; CLU_062456_3_1_6; -.
DR   OMA; HVLSKFH; -.
DR   Proteomes; UP000001217; Chromosome I.
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_1000118417"
FT   STRAND          6..12
FT                   /evidence="ECO:0007829|PDB:2MJL"
FT   HELIX           16..19
FT                   /evidence="ECO:0007829|PDB:2MJL"
FT   HELIX           25..37
FT                   /evidence="ECO:0007829|PDB:2MJL"
FT   TURN            45..47
FT                   /evidence="ECO:0007829|PDB:2MJL"
FT   STRAND          48..56
FT                   /evidence="ECO:0007829|PDB:2MJL"
FT   STRAND          59..67
FT                   /evidence="ECO:0007829|PDB:2MJL"
FT   TURN            69..71
FT                   /evidence="ECO:0007829|PDB:2MJL"
FT   HELIX           72..84
FT                   /evidence="ECO:0007829|PDB:2MJL"
FT   HELIX           88..90
FT                   /evidence="ECO:0007829|PDB:2MJL"
FT   STRAND          91..100
FT                   /evidence="ECO:0007829|PDB:2MJL"
FT   STRAND          104..110
FT                   /evidence="ECO:0007829|PDB:2MJL"
FT   HELIX           117..124
FT                   /evidence="ECO:0007829|PDB:2MJL"
FT   STRAND          133..138
FT                   /evidence="ECO:0007829|PDB:2MJL"
FT   HELIX           149..152
FT                   /evidence="ECO:0007829|PDB:2MJL"
FT   HELIX           158..180
FT                   /evidence="ECO:0007829|PDB:2MJL"
FT   HELIX           183..190
FT                   /evidence="ECO:0007829|PDB:2MJL"
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