ID   KPTA_ECOLI              Reviewed;         184 AA.
AC   P39380; Q2M5Y2;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=RNA 2'-phosphotransferase;
DE            EC=2.7.1.-;
GN   Name=kptA; Synonyms=yjiI; OrderedLocusNames=b4331, JW5784;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT   from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION.
RX   PubMed=9915792; DOI=10.1074/jbc.274.5.2637;
RA   Spinelli S.L., Kierzek R., Turner D.H., Phizicky E.M.;
RT   "Transient ADP-ribosylation of a 2'-phosphate implicated in its removal
RT   from ligated tRNA during splicing in yeast.";
RL   J. Biol. Chem. 274:2637-2644(1999).
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:0000269|PubMed:9915792}.
CC   -!- SIMILARITY: Belongs to the KptA/TPT1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA97227.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U14003; AAA97227.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC77287.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78324.1; -; Genomic_DNA.
DR   PIR; S56556; S56556.
DR   RefSeq; NP_418751.4; NC_000913.3.
DR   RefSeq; WP_001151855.1; NZ_SSZK01000015.1.
DR   AlphaFoldDB; P39380; -.
DR   SMR; P39380; -.
DR   BioGRID; 4259662; 111.
DR   BioGRID; 853138; 3.
DR   IntAct; P39380; 3.
DR   STRING; 511145.b4331; -.
DR   PaxDb; P39380; -.
DR   PRIDE; P39380; -.
DR   EnsemblBacteria; AAC77287; AAC77287; b4331.
DR   EnsemblBacteria; BAE78324; BAE78324; BAE78324.
DR   GeneID; 948858; -.
DR   KEGG; ecj:JW5784; -.
DR   KEGG; eco:b4331; -.
DR   PATRIC; fig|1411691.4.peg.2357; -.
DR   EchoBASE; EB2458; -.
DR   eggNOG; COG1859; Bacteria.
DR   HOGENOM; CLU_052998_4_0_6; -.
DR   InParanoid; P39380; -.
DR   OMA; YLYHGTV; -.
DR   PhylomeDB; P39380; -.
DR   BioCyc; EcoCyc:G7928-MON; -.
DR   PRO; PR:P39380; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:InterPro.
DR   GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IDA:EcoCyc.
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="RNA 2'-phosphotransferase"
FT                   /id="PRO_0000157476"
SQ   SEQUENCE   184 AA;  20530 MW;  2C654B7C762E7494 CRC64;
     MAKYNEKELA DTSKFLSFVL RHKPEAIGIV LDREGWADID KLILCAQKAG KRLTRALLDT
     VVATSDKKRF SYSSDGRCIR AVQGHSTSQV AISFAEKTPP QFLYHGTASR FLDEIKKQGL
     IAGERHYVHL SADEATARKV GARHGSPVIL TVKAQEMAKR GLPFWQAENG VWLTSTVAVE
     FLEW