ID PTH_BRUA2 Reviewed; 250 AA.
AC Q2YLX5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 02-NOV-2016, entry version 69.
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=BAB1_1552;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Brucellaceae; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(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; AM040264; CAJ11508.1; -; Genomic_DNA.
DR RefSeq; WP_002964641.1; NZ_KN046823.1.
DR ProteinModelPortal; Q2YLX5; -.
DR EnsemblBacteria; CAJ11508; CAJ11508; BAB1_1552.
DR GeneID; 3788869; -.
DR KEGG; bmf:BAB1_1552; -.
DR PATRIC; 17846097; VBIBruMel86222_1610.
DR HOGENOM; HOG000004797; -.
DR KO; K01056; -.
DR OMA; KSLDAHC; -.
DR PRO; PR:Q2YLX5; -.
DR Proteomes; UP000002719; 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; Reference proteome.
FT CHAIN 1 250 Peptidyl-tRNA hydrolase.
FT /FTId=PRO_0000264010.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 3 188 ipfam:Pept_tRNA_hydro [T]
FT MYHIT 107 117 ipat:PEPT_TRNA_HYDROL_2 [T]
FT MYHIT 14 27 ipat:PEPT_TRNA_HYDROL_1 [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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