KPTA_CLOP1
ID KPTA_CLOP1 Reviewed; 186 AA.
AC Q0TUT1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=CPF_0145;
OS Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS 6125 / NCTC 8237 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195103;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC Type A;
RX PubMed=16825665; DOI=10.1101/gr.5238106;
RA Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA Paulsen I.T.;
RT "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT Clostridium perfringens.";
RL Genome Res. 16:1031-1040(2006).
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; CP000246; ABG83861.1; -; Genomic_DNA.
DR RefSeq; WP_011590083.1; NC_008261.1.
DR AlphaFoldDB; Q0TUT1; -.
DR SMR; Q0TUT1; -.
DR EnsemblBacteria; ABG83861; ABG83861; CPF_0145.
DR GeneID; 29572731; -.
DR KEGG; cpf:CPF_0145; -.
DR eggNOG; COG1859; Bacteria.
DR HOGENOM; CLU_052998_4_0_9; -.
DR OMA; YLYHGTV; -.
DR OrthoDB; 1893705at2; -.
DR Proteomes; UP000001823; 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_1000022012"
SQ SEQUENCE 186 AA; 21488 MW; 541A13D0C5B24147 CRC64;
MKNNDSKISK YISLILRHKP EEIGLKLDEH GYLGVLDLIE GLNKSYEGFS MDDLERIVRE
DSKGRYSFNE DKSKIRANQG HSIKVDLGLE PIKPPKVLYH GTGRKYLESI LKNGLIKKER
NYVHLSKDIE TASIVGKRHG DLVILEVDSE SMFNDGIKFY LSKNNVWLCN YVPKKYIKEL
NLEEVF