ID   PTH2_CORGL              Reviewed;         204 AA.
AC   Q8NRV6;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, 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};
GN   OrderedLocusNames=Cgl0935, cg1067;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
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=CAF19641.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000036; BAB98328.1; -; Genomic_DNA.
DR   EMBL; BX927150; CAF19641.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_600163.1; NC_003450.3.
DR   RefSeq; WP_011013986.1; NC_006958.1.
DR   AlphaFoldDB; Q8NRV6; -.
DR   SMR; Q8NRV6; -.
DR   STRING; 196627.cg1067; -.
DR   KEGG; cgb:cg1067; -.
DR   KEGG; cgl:Cgl0935; -.
DR   PATRIC; fig|196627.13.peg.921; -.
DR   eggNOG; COG0193; Bacteria.
DR   HOGENOM; CLU_062456_4_0_11; -.
DR   OMA; SQWLGTR; -.
DR   Proteomes; UP000000582; 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; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN           1..204
FT                   /note="Peptidyl-tRNA hydrolase 2"
FT                   /id="PRO_0000187728"
SQ   SEQUENCE   204 AA;  21695 MW;  1B5611D116680C77 CRC64;
     MTSVSFLSKI QALFAPKPEL PAAKWLVVGL GNPGAKYEST RHNVGYMCQD MLIDAHQQQP
     LTPATGYKAL TTQLAPGVLA VRSTTFMNHS GQGVAPIAAA LGIPAERIIV IHDELDLPAG
     KVRLKKGGNE NGHNGLKSLT EELGTRDYLR VRIGISRPPA GMAVPDYVLE PVDHDQPGIE
     LAAEAVDLLL AQGLSAAQNA IHSR