KPTA_BURL3
ID KPTA_BURL3 Reviewed; 194 AA.
AC Q395F2;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-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};
GN OrderedLocusNames=Bcep18194_B1795;
OS Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS R18194 / 383).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=482957;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia sp. 383.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000152; ABB11909.1; -; Genomic_DNA.
DR RefSeq; WP_011355397.1; NC_007511.1.
DR AlphaFoldDB; Q395F2; -.
DR SMR; Q395F2; -.
DR EnsemblBacteria; ABB11909; ABB11909; Bcep18194_B1795.
DR GeneID; 45098130; -.
DR KEGG; bur:Bcep18194_B1795; -.
DR PATRIC; fig|482957.22.peg.5527; -.
DR HOGENOM; CLU_052998_4_0_4; -.
DR OMA; YLYHGTV; -.
DR OrthoDB; 1893705at2; -.
DR Proteomes; UP000002705; Chromosome 2.
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; Transferase.
FT CHAIN 1..194
FT /note="Probable RNA 2'-phosphotransferase"
FT /id="PRO_0000231952"
SQ SEQUENCE 194 AA; 21693 MW; CE689CD1BDB3E5B5 CRC64;
MNTKKNELPA PDATRISRTL SYLLRHAPQT IGLQLDPEGW ADIDELIAGI ARQGLHLDRA
TLETVCATND KQRFALSDDG RRIRAVQGHS TPVVQRRYPA AQPPERLYHG TATRFLDSIR
AQGLKPGARH HVHLSPDIRT ALAVGTRYGV PVILEVDAQR MHRQGHTFFV AENGVWLTDT
VPAEFLKEMD QPAR