PTH_BRUAB
ID PTH_BRUAB Reviewed; 250 AA.
AC Q9AEQ5; Q57BY1;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=BruAb1_1525;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Danese I., Haine V., Letesson J.J.;
RT "BuG, a putative GTP-binding protein essential for siderophore 2,3-
RT dihydroxybenzoic acid utilization by Brucella melitensis 16M.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(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; AY028973; AAK29776.1; -; Genomic_DNA.
DR EMBL; AE017223; AAX74853.1; -; Genomic_DNA.
DR RefSeq; WP_002964641.1; NC_006932.1.
DR AlphaFoldDB; Q9AEQ5; -.
DR SMR; Q9AEQ5; -.
DR EnsemblBacteria; AAX74853; AAX74853; BruAb1_1525.
DR GeneID; 3788869; -.
DR KEGG; bmb:BruAb1_1525; -.
DR HOGENOM; CLU_062456_1_1_5; -.
DR OMA; HVLSKFH; -.
DR PRO; PR:Q9AEQ5; -.
DR Proteomes; UP000000540; Chromosome I.
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; PS01195; PEPT_TRNA_HYDROL_1; 1.
DR PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase.
FT CHAIN 1..250
FT /note="Peptidyl-tRNA hydrolase"
FT /id="PRO_0000187704"
FT REGION 192..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 250 AA; 27568 MW; 1B6BDBB07450A4D0 CRC64;
MLLIAGLGNP GPQYAHNRHN IGFMAADEIF RRHRFSNWQK KFQAEIADGV IDGEKVLLVK
PQTFMNLSGQ SIGEAMRFYK MTPADLVVIY DELDLVPGKL RIKTGGGSGG HNGIKSIDAH
MQSFPGGQNY RRMRLGIGHP GAKELVHNYV LGDFAKADNE WLDTLMGAVA DNVAMLARRE
DNSFMNRIAL AMGDGNQRPG GVKTDPAQLE KAPPKAQSHI RQARQNQKKP NIPESGPMAE
MLKKLLGKKD
