PTH_KORVE
ID PTH_KORVE Reviewed; 201 AA.
AC Q1IHW2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 25-MAY-2022, entry version 79.
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=Acid345_4538;
OS Koribacter versatilis (strain Ellin345).
OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae;
OC Candidatus Koribacter.
OX NCBI_TaxID=204669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin345;
RX PubMed=19201974; DOI=10.1128/aem.02294-08;
RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT "Three genomes from the phylum Acidobacteria provide insight into the
RT lifestyles of these microorganisms in soils.";
RL Appl. Environ. Microbiol. 75:2046-2056(2009).
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=ABF43538.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000360; ABF43538.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041857166.1; NC_008009.1.
DR AlphaFoldDB; Q1IHW2; -.
DR SMR; Q1IHW2; -.
DR STRING; 204669.Acid345_4538; -.
DR EnsemblBacteria; ABF43538; ABF43538; Acid345_4538.
DR KEGG; aba:Acid345_4538; -.
DR eggNOG; COG0193; Bacteria.
DR HOGENOM; CLU_062456_4_1_0; -.
DR Proteomes; UP000002432; 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..201
FT /note="Peptidyl-tRNA hydrolase"
FT /id="PRO_0000263999"
FT REGION 178..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 201 AA; 21691 MW; 3D2190B47B318F48 CRC64;
MKLIVGLGNP GMQYQFTPHN LGFLAVDRIA EKYGIRVANR NCKALTGRGV IEGVDVVLAK
PETYMNLSGA SVQELVSELE IDGTKDMIVI YDDLDLPYGS IRVRERGSAG GHNGVQSIIG
ALDTQEFLRI RIGIAPEFKL SDGASYVLSQ LKKSQLPVVD QALDDAAEAV KVILREGPGP
AMNRFNRKPE PPESGGEVAA K