KPTA_RHOBA
ID KPTA_RHOBA Reviewed; 184 AA.
AC Q7UEP2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=RB11219;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294153; CAD78993.1; -; Genomic_DNA.
DR RefSeq; NP_869850.1; NC_005027.1.
DR RefSeq; WP_007329713.1; NC_005027.1.
DR AlphaFoldDB; Q7UEP2; -.
DR SMR; Q7UEP2; -.
DR STRING; 243090.RB11219; -.
DR EnsemblBacteria; CAD78993; CAD78993; RB11219.
DR KEGG; rba:RB11219; -.
DR PATRIC; fig|243090.15.peg.5430; -.
DR eggNOG; COG1859; Bacteria.
DR HOGENOM; CLU_052998_4_0_0; -.
DR InParanoid; Q7UEP2; -.
DR OMA; YLYHGTV; -.
DR OrthoDB; 1893705at2; -.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:InterPro.
DR GO; GO:0000215; F:tRNA 2'-phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
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_0000226045"
SQ SEQUENCE 184 AA; 20423 MW; BD573515F7032E02 CRC64;
MKADKQLVST SKFLSLVLRH QPGVIGMTLD EQGWLEIDGL IANANTRGKK LTLELIHEVV
ATNDKKRFVL SDDGLRIRAS QGHSVAGVDL NLTEANPPAT LYHGTVDAFL PRIREQGLQK
RSRNHVHLSA DEATATNVGS RRGKPKLLLI AAQRMHQDGH IFYLSENEVW LVDSVPPTYL
TFPT