ID PTH2_CORJK Reviewed; 240 AA.
AC Q4JU38;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=Peptidyl-tRNA hydrolase 2 {ECO:0000255|HAMAP-Rule:MF_00083};
DE Short=PTH 2 {ECO:0000255|HAMAP-Rule:MF_00083};
DE EC=3.1.1.29 {ECO:0000255|HAMAP-Rule:MF_00083};
GN Name=pth2 {ECO:0000255|HAMAP-Rule:MF_00083}; OrderedLocusNames=jk1496;
OS Corynebacterium jeikeium (strain K411).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; 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}.
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DR EMBL; CR931997; CAI37669.1; -; Genomic_DNA.
DR RefSeq; WP_005293388.1; NC_007164.1.
DR AlphaFoldDB; Q4JU38; -.
DR SMR; Q4JU38; -.
DR STRING; 306537.jk1496; -.
DR GeneID; 3432995; -.
DR KEGG; cjk:jk1496; -.
DR eggNOG; COG0193; Bacteria.
DR HOGENOM; CLU_062456_4_0_11; -.
DR OrthoDB; 9800507at2; -.
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; Peptidyl-tRNA hydrolase; 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 NCBIfam; TIGR00447; pth; 1.
DR PANTHER; PTHR17224; PEPTIDYL-TRNA HYDROLASE; 1.
DR PANTHER; PTHR17224:SF1; PEPTIDYL-TRNA HYDROLASE-RELATED; 1.
DR Pfam; PF01195; Pept_tRNA_hydro; 1.
DR SUPFAM; SSF53178; Peptidyl-tRNA hydrolase-like; 1.
DR PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..240
FT /note="Peptidyl-tRNA hydrolase 2"
FT /id="PRO_0000264026"
SQ SEQUENCE 240 AA; 26242 MW; 5FACA1DD8B825B7C CRC64;
MAVSFLQSLF SVFRKKSSPQ EPATTTAGGP AKRTKLTVGE LQEFAPEWIV IGLGNPGAKY
ADTRHNIGYW PIDRLVERYE AQWLPVEGQK AHAALITVEE TPVLLLRSTT YMNNSGEAVG
PLASALSLPA ERIIVCHDEL DIAAGQVRIK DKGGEGGHNG LRSMTAELGT QHYVRVRMGI
GRPPKGTSVI DFVLSPFEEA DIDAENGWME NTLRDSVDSV TLIVNNGTDI ARNDIHTRKH
//
