ID E4TBW3_RIEAD Unreviewed; 187 AA.
AC E4TBW3;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 61.
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 ORFNames=RA0C_1095 {ECO:0000313|EMBL:AFD56012.1};
OS Riemerella anatipestifer (strain ATCC 11845 / DSM 15868 / JCM 9532 / NCTC
OS 11014).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Riemerella.
OX NCBI_TaxID=693978 {ECO:0000313|EMBL:AFD56012.1, ECO:0000313|Proteomes:UP000010093};
RN [1] {ECO:0000313|EMBL:AFD56012.1, ECO:0000313|Proteomes:UP000010093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15868 {ECO:0000313|Proteomes:UP000010093};
RX PubMed=22628503; DOI=10.1128/JB.00366-12;
RA Wang X., Zhu D., Wang M., Cheng A., Jia R., Zhou Y., Chen Z., Luo Q.,
RA Liu F., Wang Y., Chen X.Y.;
RT "Complete genome sequence of Riemerella anatipestifer reference strain.";
RL J. Bacteriol. 194:3270-3271(2012).
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; CP003388; AFD56012.1; -; Genomic_DNA.
DR RefSeq; WP_004918128.1; NC_017045.1.
DR AlphaFoldDB; E4TBW3; -.
DR GeneID; 66848542; -.
DR KEGG; rai:RA0C_1095; -.
DR KEGG; ran:Riean_0848; -.
DR PATRIC; fig|693978.17.peg.1094; -.
DR HOGENOM; CLU_062456_4_1_10; -.
DR Proteomes; UP000010093; 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; 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.
DR PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 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 187 AA; 21038 MW; 6E0215A4D3BA94DB CRC64;
MKYLIVGLGN KGDEYTETRH NVGFKVVEKI AEGIEAPFKT ANFGWVAEGK YKGRKVILLK
PDTYMNLSGN AVKFWLKKEN IPLENLLVIT DDLALPFGTL RMKMKGSDAG HNGLKNIQEL
LQTQNYPRLR FGISANFSEG KQVDYVLGKW TEEEQSKLPE RLEQFTKASL AFVFAGIQNA
MTGFNGK
//
