MODA_BPT4
ID MODA_BPT4 Reviewed; 200 AA.
AC P39421;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=NAD--protein ADP-ribosyltransferase modA {ECO:0000255|HAMAP-Rule:MF_04141};
DE EC=2.4.2.31 {ECO:0000255|HAMAP-Rule:MF_04141, ECO:0000269|PubMed:10634320, ECO:0000269|PubMed:15489438};
DE AltName: Full=RNA polymerase ADP-ribosylase modA {ECO:0000255|HAMAP-Rule:MF_04141};
GN Name=modA {ECO:0000255|HAMAP-Rule:MF_04141};
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9193638; DOI=10.1007/978-1-4419-8632-0_8;
RA Wilkens K., Tiemann B., Bazan J.F., Rueger W.;
RT "ADP-ribosylation and early transcription regulation by bacteriophage T4.";
RL Adv. Exp. Med. Biol. 419:71-82(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT "Bacteriophage T4 genome.";
RL Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN [3]
RP FUNCTION.
RX PubMed=7031602; DOI=10.1093/nar/9.19.4863;
RA Goldfarb A., Palm P.;
RT "Control of promoter utilization by bacteriophage T4-induced modification
RT of RNA polymerase alpha subunit.";
RL Nucleic Acids Res. 9:4863-4878(1981).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10634320;
RA Tiemann B., Depping R., Rueger W.;
RT "Overexpression, purification, and partial characterization of ADP-
RT ribosyltransferases modA and modB of bacteriophage T4.";
RL Gene Expr. 8:187-196(1999).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-72; SER-109; GLN-116;
RP PHE-127; ASN-128; PHE-129; GLU-163; GLN-164 AND GLU-165, AND ACTIVE SITE.
RX PubMed=15489438; DOI=10.1128/jb.186.21.7262-7272.2004;
RA Tiemann B., Depping R., Gineikiene E., Kaliniene L., Nivinskas R.,
RA Ruger W.;
RT "ModA and ModB, two ADP-ribosyltransferases encoded by bacteriophage T4:
RT catalytic properties and mutation analysis.";
RL J. Bacteriol. 186:7262-7272(2004).
CC -!- FUNCTION: ADP-ribosyltransferase that efficiently ADP-ribosylates both
CC alpha subunits of host RNA polymerase RPOA (PubMed:15489438,
CC PubMed:10634320). The ModA-induced ADP-ribosylation of RPOA alpha
CC subunits inhibits transcription from viral early promoters
CC (PubMed:7031602). {ECO:0000255|HAMAP-Rule:MF_04141,
CC ECO:0000269|PubMed:10634320, ECO:0000269|PubMed:15489438,
CC ECO:0000269|PubMed:7031602}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-
CC ribosyl)-L-arginyl-[protein] + nicotinamide; Xref=Rhea:RHEA:19149,
CC Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142554; EC=2.4.2.31; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_04141, ECO:0000269|PubMed:10634320,
CC ECO:0000269|PubMed:15489438};
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04141}.
CC Note=This protein is injected from the virion into the bacterial cell.
CC {ECO:0000255|HAMAP-Rule:MF_04141}.
CC -!- SIMILARITY: Belongs to the Tevenvirinae NAD--protein ADP-
CC ribosyltransferase modA family. {ECO:0000255|HAMAP-Rule:MF_04141}.
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DR EMBL; X98695; CAA67255.1; -; Genomic_DNA.
DR EMBL; M30001; AAB07802.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42601.1; -; Genomic_DNA.
DR PIR; T10143; T10143.
DR RefSeq; NP_049635.1; NC_000866.4.
DR GeneID; 1258568; -.
DR KEGG; vg:1258568; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0044423; C:virion component; IEA:UniProtKB-UniRule.
DR GO; GO:0106274; F:NAD+-protein-arginine ADP-ribosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0070213; P:protein auto-ADP-ribosylation; IDA:CACAO.
DR HAMAP; MF_04141; MODA_T4; 1.
DR InterPro; IPR043663; MODA-like.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Reference proteome; Transferase; Virion.
FT CHAIN 1..200
FT /note="NAD--protein ADP-ribosyltransferase modA"
FT /id="PRO_0000164955"
FT ACT_SITE 165
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04141,
FT ECO:0000269|PubMed:15489438"
FT BINDING 72
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04141,
FT ECO:0000269|PubMed:15489438"
FT MUTAGEN 72
FT /note="R->A: Complete loss of enzymatic activity in vitro."
FT /evidence="ECO:0000269|PubMed:15489438"
FT MUTAGEN 109
FT /note="S->A: Complete loss of enzymatic activity in vitro."
FT /evidence="ECO:0000269|PubMed:15489438"
FT MUTAGEN 116
FT /note="Q->A: No effect on enzymatic activity in vitro."
FT /evidence="ECO:0000269|PubMed:15489438"
FT MUTAGEN 127
FT /note="F->A: Complete loss of enzymatic activity in vitro."
FT /evidence="ECO:0000269|PubMed:15489438"
FT MUTAGEN 128
FT /note="N->A: No effect on enzymatic activity in vitro."
FT /evidence="ECO:0000269|PubMed:15489438"
FT MUTAGEN 129
FT /note="F->A: Complete loss of enzymatic activity in vitro."
FT /evidence="ECO:0000269|PubMed:15489438"
FT MUTAGEN 163
FT /note="E->A: Complete loss of enzymatic activity in vitro."
FT /evidence="ECO:0000269|PubMed:15489438"
FT MUTAGEN 164
FT /note="Q->A: No effect on enzymatic activity in vitro."
FT /evidence="ECO:0000269|PubMed:15489438"
FT MUTAGEN 165
FT /note="E->A: Complete loss of enzymatic activity in vitro."
FT /evidence="ECO:0000269|PubMed:15489438"
SQ SEQUENCE 200 AA; 23348 MW; 2AD2150D11790B52 CRC64;
MKYSVMQLKD FKIKSMDASV RASIREELLS EGFNLSEIEL LIHCITNKPD DHSWLNEIIK
SRLVPNDKPL WRGVPAETKQ VLNQGIDIIT FDKVVSASYD KNIALHFASG LEYNTQVIFE
FKAPMVFNFQ EYAIKALRCK EYNPNFKFPD SHRYRNMELV SDEQEVMIPA GSVFRIADRY
EYKKCSTYTI YTLDFEGFNL
