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 02-NOV-2016, 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};
GN OrderedLocusNames=BruAb1_1525;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Brucellaceae; 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.,
RA Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison
RT to the highly similar genomes of Brucella melitensis and Brucella
RT suis.";
RL J. Bacteriol. 187:2715-2726(2005).
CC -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-
CC tRNAs which drop off the ribosome during protein synthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00083}.
CC -!- CATALYTIC ACTIVITY: N-substituted aminoacyl-tRNA + H(2)O = N-
CC substituted amino acid + tRNA. {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}.
DR EMBL; AY028973; AAK29776.1; -; Genomic_DNA.
DR EMBL; AE017223; AAX74853.1; -; Genomic_DNA.
DR RefSeq; WP_002964641.1; NC_006932.1.
DR ProteinModelPortal; Q9AEQ5; -.
DR EnsemblBacteria; AAX74853; AAX74853; BruAb1_1525.
DR GeneID; 3788869; -.
DR KEGG; bmb:BruAb1_1525; -.
DR PATRIC; 17824798; VBIBruAbo15061_1613.
DR HOGENOM; HOG000004797; -.
DR KO; K01056; -.
DR OMA; KSLDAHC; -.
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-HAMAP.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP.
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 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 Complete proteome; Cytoplasm; Hydrolase.
FT CHAIN 1 250 Peptidyl-tRNA hydrolase.
FT /FTId=PRO_0000187704.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 107 117 ipat:PEPT_TRNA_HYDROL_2 [T]
FT MYHIT 14 27 ipat:PEPT_TRNA_HYDROL_1 [T]
FT MYHIT 3 188 ipfam:Pept_tRNA_hydro [T]
FT MYHIT 1 182 ihamap:Pept_tRNA_hydro_bact [T]
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
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