ID   ALT_BPT2                Reviewed;         698 AA.
AC   Q38424;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=NAD(+)--arginine ADP-ribosyltransferase {ECO:0000255|HAMAP-Rule:MF_04139};
DE            EC=2.4.2.31 {ECO:0000255|HAMAP-Rule:MF_04139};
DE   AltName: Full=Alt protein {ECO:0000303|PubMed:8053153};
DE   Flags: Precursor;
GN   Name=alt;
OS   Enterobacteria phage T2 (Bacteriophage T2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX   NCBI_TaxID=10664;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION.
RC   STRAIN=WT;
RX   PubMed=8053153; DOI=10.1006/viro.1994.1487;
RA   Koch T., Rueger W.;
RT   "The ADP-ribosyltransferases (gpAlt) of bacteriophages T2, T4, and T6:
RT   sequencing of the genes and comparison of their products.";
RL   Virology 203:294-298(1994).
CC   -!- FUNCTION: ADP-ribosyltransferase that efficiently ADP-ribosylates one
CC       of the two alpha subunits of host RNA polymerase RPOA on an arginine
CC       located in the C-terminal region. ADP-ribosylation of RPOA alpha
CC       subunit enhances the transcription of viral early genes. Also
CC       ribosylates RPOA subunits beta, beta' and sigma 70 and performs an
CC       autoribosylation reaction. {ECO:0000255|HAMAP-Rule:MF_04139}.
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_04139};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19150;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_04139};
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04139}.
CC       Note=About 25-50 copies per virion. This protein is injected into the
CC       bacterial cell along with the viral DNA. {ECO:0000255|HAMAP-
CC       Rule:MF_04139}.
CC   -!- SIMILARITY: Belongs to the Tevenvirinae NAD(+)--arginine ADP-
CC       ribosyltransferase family. {ECO:0000255|HAMAP-Rule:MF_04139}.
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DR   EMBL; X69893; CAA49517.1; -; Genomic_DNA.
DR   PIR; S31630; S31630.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0044423; C:virion component; IEA:UniProtKB-UniRule.
DR   GO; GO:0106274; F:NAD+-protein-arginine ADP-ribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046782; P:regulation of viral transcription; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04139; ALT_T4; 1.
DR   InterPro; IPR003540; ADP-ribosyltransferase.
DR   InterPro; IPR016225; Phage_T4_Alt-like.
DR   Pfam; PF03496; ADPrib_exo_Tox; 1.
DR   PIRSF; PIRSF000491; Alt_phage; 1.
DR   PROSITE; PS51996; TR_MART; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; NAD; Nucleotidyltransferase; Transferase; Virion.
FT   PROPEP          1..7
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04139"
FT                   /id="PRO_0000447618"
FT   CHAIN           8..698
FT                   /note="NAD(+)--arginine ADP-ribosyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04139"
FT                   /id="PRO_0000164916"
FT   DOMAIN          375..628
FT                   /note="TR mART core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        481
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        506
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   ACT_SITE        590
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   SITE            7..8
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04139"
SQ   SEQUENCE   698 AA;  77997 MW;  B2D0BAEB729457C6 CRC64;
     MMELITELFD EDTTLPITNL NPKKKIPQIF SVHVDDAIEQ PGFRLCTYTS GGDTNRDLKM
     GDKMMHIVPF TLTAKGSIAK LKGLGPSPIN YINSVFTVAM QTMRQYKIDA CMLRILKSKT
     AGQARQIQVI ADRLIRSRSG GRYVLLKELW DYDKKYAYIL IHRKNVSLED IPGVPEISTE
     LFTKVESKVG DVYINKDTGA QVTKNEAIAA SIAQENDKRT DQAVIVKVKI SRRAIAQSQS
     LESSRFESEL FQKYESTAAN FNKPATAPLI PEAEEMKIGI NSLASKTKAA KIIAEGTANE
     LHYDYKFFSK SEVDEVSEKI KDVIFNAIKN EPTTSIKCLE KYAAAVNQFF EEYKDNWLDK
     HNKTRKGQPD EVWGEITKNA WNAAKTKFLK RMIYSFSGIG AGPMIDITIA CDGSKYTPSQ
     KRGIREYCGS GYTDINNLLL GRYNPERYDV MSEKEIESAI NNLDSAFENG DRIPEGITVY
     RAQSMTAPIY EALVKNKVFY FRNFVSTSLT PIIFGRFGIT HAGIGLLEPE ARNELTVDKN
     EEGITINPNE IRAYKENPEY VKVQIGWAID GAHKVNVVYP GSLGIATEAE VILPRGLMVK
     VNKITDASNN DGTTSNNTKL IQAEVMTTEE LTESVIYDGD RLMETGEVVA MTGDIEIEDR
     VDFASFVSSN VKQKVESSLG IIASCIDITN MPYKFVQG