KPTA_ACET2
ID KPTA_ACET2 Reviewed; 182 AA.
AC A3DJX6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Cthe_3059;
OS Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC
OS 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=203119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL
RC B-4536 / VPI 7372;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Wu J.H.D.,
RA Newcomb M., Richardson P.;
RT "Complete sequence of Clostridium thermocellum ATCC 27405.";
RL Submitted (FEB-2007) 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; CP000568; ABN54255.1; -; Genomic_DNA.
DR PDB; 6E3A; X-ray; 1.40 A; A=1-182.
DR PDB; 6EDE; X-ray; 1.55 A; A=1-182.
DR PDBsum; 6E3A; -.
DR PDBsum; 6EDE; -.
DR AlphaFoldDB; A3DJX6; -.
DR SMR; A3DJX6; -.
DR STRING; 203119.Cthe_3059; -.
DR EnsemblBacteria; ABN54255; ABN54255; Cthe_3059.
DR KEGG; cth:Cthe_3059; -.
DR eggNOG; COG1859; Bacteria.
DR HOGENOM; CLU_052998_4_1_9; -.
DR OMA; YLYHGTV; -.
DR BRENDA; 2.7.1.160; 1530.
DR Proteomes; UP000002145; 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 1: Evidence at protein level;
KW 3D-structure; NAD; Reference proteome; Transferase.
FT CHAIN 1..182
FT /note="Probable RNA 2'-phosphotransferase"
FT /id="PRO_1000022014"
FT HELIX 6..18
FT /evidence="ECO:0007829|PDB:6E3A"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:6E3A"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:6E3A"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:6E3A"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:6E3A"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:6E3A"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:6E3A"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:6E3A"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:6E3A"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:6E3A"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:6E3A"
FT STRAND 121..129
FT /evidence="ECO:0007829|PDB:6E3A"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:6E3A"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:6E3A"
FT HELIX 151..156
FT /evidence="ECO:0007829|PDB:6E3A"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:6E3A"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:6E3A"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:6E3A"
SQ SEQUENCE 182 AA; 21113 MW; 78AA3F6EC464B2E8 CRC64;
MVLIDYSKLS KEVAYALRHA PWEYGLELDA EGWVDINQLL SSLHECEKWK KVSEHDLHVM
IEKSDKKRYE ISNGKIRALY GHSIPQRIIK EQKCPPEVLY HGTARRFVKS IKEKGLQPQG
RQYVHLSADV ETALQVGKRR DIKPVLLIVN ALEAWSEGIK FYLGNDKVWL ADAIPSKYIR
FE
