ID   PTH1_CORJK              Reviewed;         193 AA.
AC   Q4JU39;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Peptidyl-tRNA hydrolase 1 {ECO:0000255|HAMAP-Rule:MF_00083};
DE            Short=PTH 1 {ECO:0000255|HAMAP-Rule:MF_00083};
DE            EC=3.1.1.29 {ECO:0000255|HAMAP-Rule:MF_00083};
GN   Name=pth1 {ECO:0000255|HAMAP-Rule:MF_00083}; OrderedLocusNames=jk1495;
OS   Corynebacterium jeikeium (strain K411).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=306537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K411;
RX   PubMed=15968079; DOI=10.1128/jb.187.13.4671-4682.2005;
RA   Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA   Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA   Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT   "Complete genome sequence and analysis of the multiresistant nosocomial
RT   pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT   human skin flora.";
RL   J. Bacteriol. 187:4671-4682(2005).
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAI37668.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR931997; CAI37668.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q4JU39; -.
DR   SMR; Q4JU39; -.
DR   STRING; 306537.jk1495; -.
DR   EnsemblBacteria; CAI37668; CAI37668; jk1495.
DR   KEGG; cjk:jk1495; -.
DR   PATRIC; fig|306537.10.peg.1515; -.
DR   eggNOG; COG0193; Bacteria.
DR   HOGENOM; CLU_062456_2_2_11; -.
DR   Proteomes; UP000000545; 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; PS01196; PEPT_TRNA_HYDROL_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN           1..193
FT                   /note="Peptidyl-tRNA hydrolase 1"
FT                   /id="PRO_0000264025"
SQ   SEQUENCE   193 AA;  20691 MW;  8DC188BFC3D5E8B9 CRC64;
     MASPNKKQHT NSDTWLIVGL GNPGDKYANT RHNVGRMVIG ELLDRQVPAA SLNTHKKTNT
     DIAEVKIAGR KVVLAQPRTF MNVSGGPVQQ LAAFFKIPAE NIIVAYDDLE GDPGAVKLRQ
     SGGDKGHNGL KSITKSLGTK DYWRLSCGIG RPPGRMDPAA YVLKPFPKSE AAEVAIMCAD
     AADEVERTLG VGN