ID   KPTA_PECCP              Reviewed;         186 AA.
AC   C6DJM6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 60.
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=PC1_0381;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) 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; CP001657; ACT11439.1; -; Genomic_DNA.
DR   RefSeq; WP_012773096.1; NC_012917.1.
DR   AlphaFoldDB; C6DJM6; -.
DR   SMR; C6DJM6; -.
DR   STRING; 561230.PC1_0381; -.
DR   EnsemblBacteria; ACT11439; ACT11439; PC1_0381.
DR   KEGG; pct:PC1_0381; -.
DR   eggNOG; COG1859; Bacteria.
DR   HOGENOM; CLU_052998_4_0_6; -.
DR   OMA; YLYHGTV; -.
DR   OrthoDB; 1893705at2; -.
DR   Proteomes; UP000002736; Chromosome.
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..186
FT                   /note="Probable RNA 2'-phosphotransferase"
FT                   /id="PRO_1000204944"
SQ   SEQUENCE   186 AA;  20565 MW;  05ED552089F8C2A8 CRC64;
     MSNTKHADVS KFLSYVLRHK PEAIGLTLNS GGWANIAELI SCAAKDGRLL TREVIQSVVD
     NSDKKRFSIS ADGLSIRAAQ GHSSAQVDMR YEPKVPPEFL YHGTATRFID SINQQGLRPG
     SRQYVHLSAD EATAITVGQR HGKPTVLKIK TLEMHQQGFI FYQADNGVWL TLTVPVPFID
     STPFID