ID   KPTA_STRCO              Reviewed;         182 AA.
AC   Q9ZBX9;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Probable RNA 2'-phosphotransferase;
DE            EC=2.7.1.-;
GN   Name=kptA; OrderedLocusNames=SCO3953; ORFNames=SCD78.20c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the KptA/TPT1 family. {ECO:0000305}.
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DR   EMBL; AL939118; CAA22225.1; -; Genomic_DNA.
DR   PIR; T36059; T36059.
DR   RefSeq; NP_628137.1; NC_003888.3.
DR   RefSeq; WP_011029338.1; NZ_VNID01000003.1.
DR   AlphaFoldDB; Q9ZBX9; -.
DR   SMR; Q9ZBX9; -.
DR   STRING; 100226.SCO3953; -.
DR   GeneID; 1099389; -.
DR   KEGG; sco:SCO3953; -.
DR   PATRIC; fig|100226.15.peg.4025; -.
DR   eggNOG; COG1859; Bacteria.
DR   HOGENOM; CLU_052998_4_0_11; -.
DR   OMA; YLYHGTV; -.
DR   PhylomeDB; Q9ZBX9; -.
DR   Proteomes; UP000001973; 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..182
FT                   /note="Probable RNA 2'-phosphotransferase"
FT                   /id="PRO_0000157483"
SQ   SEQUENCE   182 AA;  20415 MW;  7E0A8F9DFAB9EE81 CRC64;
     MQQERTVKVS KYLSKHLRHQ PERIGLTPDE GGWVEIDALV AAAAAHGFPF TRQELDHVVA
     TNDKRRFAVE GTRIRASQGH SIAVDLRLPV ATPPPYLYHG TVARHLEAIR AEGLRPMNRH
     DVHLSPDRET ATRVGARRGR PVVLPVDAAT MHRDGHVFHV SANGVWLTQH VPSRYLRFPA
     PH