ID   KPTA_FUSNN              Reviewed;         179 AA.
AC   Q8R5N7;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=FN1102;
OS   Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS   BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX   NCBI_TaxID=190304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC   2640 / LMG 13131 / VPI 4355;
RX   PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA   Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA   Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA   Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA   Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA   Overbeek R.;
RT   "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT   strain ATCC 25586.";
RL   J. Bacteriol. 184:2005-2018(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.
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; AE009951; AAL95298.1; -; Genomic_DNA.
DR   RefSeq; NP_603999.1; NC_003454.1.
DR   AlphaFoldDB; Q8R5N7; -.
DR   SMR; Q8R5N7; -.
DR   STRING; 190304.FN1102; -.
DR   EnsemblBacteria; AAL95298; AAL95298; FN1102.
DR   KEGG; fnu:FN1102; -.
DR   PATRIC; fig|190304.8.peg.1667; -.
DR   eggNOG; COG1859; Bacteria.
DR   HOGENOM; CLU_052998_4_0_0; -.
DR   InParanoid; Q8R5N7; -.
DR   OMA; YLYHGTV; -.
DR   BioCyc; FNUC190304:G1FZS-1682-MON; -.
DR   BRENDA; 2.7.1.160; 11865.
DR   Proteomes; UP000002521; 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..179
FT                   /note="Probable RNA 2'-phosphotransferase"
FT                   /id="PRO_0000157480"
SQ   SEQUENCE   179 AA;  20859 MW;  7C16B392037396EA CRC64;
     MDNDVKLGRF ISLILRHKPE TINLKLDKNG WANTKELIEK ISKSGREIDF EILERIVNEN
     NKKRYSFNED KTKIRAVQGH SIEVNLELKE VVPPAILYHG TAFKTLESIK KEGIKKMSRQ
     HVHLSADIET AKNVATRHSG KYIILEIDTE AMLKENYKFY LSENKVWLTD FVPSKFIKF