KPTA_BURPS
ID KPTA_BURPS Reviewed; 184 AA.
AC Q63WX9;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Probable RNA 2'-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00299};
DE EC=2.7.1.- {ECO:0000255|HAMAP-Rule:MF_00299};
GN Name=kptA {ECO:0000255|HAMAP-Rule:MF_00299}; OrderedLocusNames=BPSL0762;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC -!- FUNCTION: Removes the 2'-phosphate from RNA via an intermediate in
CC which the phosphate is ADP-ribosylated by NAD followed by a presumed
CC transesterification to release the RNA and generate ADP-ribose 1''-2''-
CC cyclic phosphate (APPR>P). May function as an ADP-ribosylase.
CC {ECO:0000255|HAMAP-Rule:MF_00299}.
CC -!- SIMILARITY: Belongs to the KptA/TPT1 family. {ECO:0000255|HAMAP-
CC Rule:MF_00299}.
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DR EMBL; BX571965; CAH34754.1; -; Genomic_DNA.
DR RefSeq; WP_011204889.1; NZ_CP009538.1.
DR RefSeq; YP_107387.1; NC_006350.1.
DR AlphaFoldDB; Q63WX9; -.
DR SMR; Q63WX9; -.
DR STRING; 272560.BPSL0762; -.
DR EnsemblBacteria; CAH34754; CAH34754; BPSL0762.
DR KEGG; bps:BPSL0762; -.
DR PATRIC; fig|272560.51.peg.847; -.
DR eggNOG; COG1859; Bacteria.
DR OMA; YLYHGTV; -.
DR Proteomes; UP000000605; Chromosome 1.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:InterPro.
DR GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:UniProtKB-UniRule.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.970; -; 1.
DR Gene3D; 3.20.170.30; -; 1.
DR HAMAP; MF_00299; KptA; 1.
DR InterPro; IPR002745; Ptrans_KptA/Tpt1.
DR InterPro; IPR042081; RNA_2'-PTrans_C.
DR InterPro; IPR022928; RNA_2'-PTrans_KptA.
DR InterPro; IPR042080; RNA_2'-PTrans_N.
DR PANTHER; PTHR12684; PTHR12684; 1.
DR Pfam; PF01885; PTS_2-RNA; 1.
PE 3: Inferred from homology;
KW NAD; Reference proteome; Transferase.
FT CHAIN 1..184
FT /note="Probable RNA 2'-phosphotransferase"
FT /id="PRO_0000231951"
SQ SEQUENCE 184 AA; 20378 MW; EC4D356963B8237B CRC64;
MSSSYFIATR ASKFLSYVLR HRPDSIGVTL DAQGWADVSE LLTKAAAAGM ALTLDELKQV
VAENDKKRFV LNDDATRIRA AQGHSVDVDL QLPVKAPPPV LYHGTVGKSM ADIRKQGLTP
MNRHDVHLSP DRETATRVAT RRGKPVILVI ETYPLLRDGY QFRVSDNGVW LVPEVPAKYI
KFPG