ID B0T898_CAUSK Unreviewed; 208 AA.
AC B0T898;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000256|ARBA:ARBA00013260, ECO:0000256|HAMAP-Rule:MF_00083};
DE Short=PTH {ECO:0000256|HAMAP-Rule:MF_00083};
DE EC=3.1.1.29 {ECO:0000256|ARBA:ARBA00013260, ECO:0000256|HAMAP-Rule:MF_00083};
GN Name=pth {ECO:0000256|HAMAP-Rule:MF_00083};
GN OrderedLocusNames=Caul_0666 {ECO:0000313|EMBL:ABZ69799.1};
OS Caulobacter sp. (strain K31).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=366602 {ECO:0000313|EMBL:ABZ69799.1};
RN [1] {ECO:0000313|EMBL:ABZ69799.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K31 {ECO:0000313|EMBL:ABZ69799.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Stephens C., Richardson P.;
RT "Complete sequence of chromosome of Caulobacter sp. K31.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs
CC which drop off the ribosome during protein synthesis.
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_00083,
CC ECO:0000256|RuleBase:RU000673};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00083}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00083}.
CC -!- SIMILARITY: Belongs to the PTH family. {ECO:0000256|ARBA:ARBA00038063,
CC ECO:0000256|HAMAP-Rule:MF_00083, ECO:0000256|RuleBase:RU004320}.
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DR EMBL; CP000927; ABZ69799.1; -; Genomic_DNA.
DR AlphaFoldDB; B0T898; -.
DR STRING; 366602.Caul_0666; -.
DR KEGG; cak:Caul_0666; -.
DR eggNOG; COG0193; Bacteria.
DR HOGENOM; CLU_062456_1_0_5; -.
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; PS01195; PEPT_TRNA_HYDROL_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00083};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00083}.
SQ SEQUENCE 208 AA; 22670 MW; 9342E5428AD8AD10 CRC64;
MSMLILAGLG NPEPKYEKNR HNVGFMAVDA LARKWGVAPW RSRFQGLACE GQVSTPNGPV
KLLLLKPKTF YNESGRAVGE AMKFFKLSPA DVIVFHDEID MAPGRFRMKA GGGAAGNNGV
RSITSQIGDG FRRGRIGVGH PGHKDAVMHY VLGDFHKVEH QWLDPLLDAV CDALPFAAAG
DDERYQAEVL RLAPAPKADP KKAARQPE
//
