ALT_BPT4
ID ALT_BPT4 Reviewed; 682 AA.
AC P12726;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 93.
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, ECO:0000269|PubMed:16112649, ECO:0000269|PubMed:173540};
DE AltName: Full=Alt protein {ECO:0000303|PubMed:8053153};
DE Flags: Precursor;
GN Name=alt;
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].
RC STRAIN=C;
RX PubMed=2506526; DOI=10.1093/nar/17.16.6731;
RA Hilse D., Koch T., Rueger W.;
RT "Nucleotide sequence of the alt gene of bacteriophage T4.";
RL Nucleic Acids Res. 17:6731-6731(1989).
RN [2]
RP SEQUENCE REVISION, AND PROTEOLYTIC CLEAVAGE.
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).
RN [3]
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 [4]
RP SUBCELLULAR LOCATION.
RX PubMed=4615179; DOI=10.1016/0022-2836(74)90537-3;
RA Horvitz H.R.;
RT "Bacteriophage T4 mutants deficient in alteration and modification of the
RT Escherichia coli RNA polymerase.";
RL J. Mol. Biol. 90:739-750(1974).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=376872; DOI=10.1128/jvi.29.3.1232-1234.1979;
RA Goff C.G.;
RT "Bacteriophage T4 alt gene maps between genes 30 and 54.";
RL J. Virol. 29:1232-1234(1979).
RN [6]
RP FUNCTION.
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=173540; DOI=10.1111/j.1432-1033.1975.tb20995.x;
RA Rohrer H., Zillig W., Mailhammer R.;
RT "ADP-ribosylation of DNA-dependent RNA polymerase of Escherichia coli by an
RT NAD+: protein ADP-ribosyltransferase from bacteriophage T4.";
RL Eur. J. Biochem. 60:227-238(1975).
RN [8]
RP FUNCTION.
RX PubMed=11021939; DOI=10.1099/00221287-146-10-2643;
RA Sommer N., Salniene V., Gineikiene E., Nivinskas R., Rueger W.;
RT "T4 early promoter strength probed in vivo with unribosylated and ADP-
RT ribosylated Escherichia coli RNA polymerase: a mutation analysis.";
RL Microbiology 146:2643-2653(2000).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16112649; DOI=10.1016/j.bbrc.2005.08.023;
RA Depping R., Lohaus C., Meyer H.E., Ruger W.;
RT "The mono-ADP-ribosyltransferases Alt and ModB of bacteriophage T4: target
RT proteins identified.";
RL Biochem. Biophys. Res. Commun. 335:1217-1223(2005).
RN [10]
RP FUNCTION.
RX PubMed=26395283; DOI=10.1111/mmi.13225;
RA Alawneh A.M., Qi D., Yonesaki T., Otsuka Y.;
RT "An ADP-ribosyltransferase Alt of bacteriophage T4 negatively regulates the
RT Escherichia coli MazF toxin of a toxin-antitoxin module.";
RL Mol. Microbiol. 99:188-198(2016).
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 (PubMed:16112649, PubMed:173540). ADP-
CC ribosylation of RPOA alpha subunit enhances the transcription of viral
CC early genes (PubMed:11021939). Also ribosylates RPOA subunits beta,
CC beta' and sigma 70 and performs an autoribosylation reaction
CC (PubMed:9193638, PubMed:173540). Additional in-vitro identified targets
CC include proteins involved in either translation or cellular metabolism
CC such as elongation factor-Tu or GroeL (PubMed:16112649). Mono-ADP-
CC ribosylates host MAZF which may inactivate the latter
CC (PubMed:26395283). {ECO:0000255|HAMAP-Rule:MF_04139,
CC ECO:0000269|PubMed:11021939, ECO:0000269|PubMed:16112649,
CC ECO:0000269|PubMed:173540, ECO:0000269|PubMed:26395283,
CC ECO:0000269|PubMed:9193638}.
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, ECO:0000269|PubMed:16112649,
CC ECO:0000269|PubMed:173540};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19150;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04139,
CC ECO:0000269|PubMed:173540};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:173540};
CC Temperature dependence:
CC Optimum temperature is 20 degrees Celsius.
CC {ECO:0000269|PubMed:173540};
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04139,
CC ECO:0000269|PubMed:376872, ECO:0000269|PubMed:4615179}. Note=About 25-
CC 50 copies per virion. This protein is injected into the bacterial cell
CC along with the viral DNA. {ECO:0000255|HAMAP-Rule:MF_04139,
CC ECO:0000269|PubMed:376872, ECO:0000269|PubMed:4615179}.
CC -!- SIMILARITY: Belongs to the Tevenvirinae NAD(+)--arginine ADP-
CC ribosyltransferase family. {ECO:0000255|HAMAP-Rule:MF_04139}.
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DR EMBL; X15811; CAA33807.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42533.1; -; Genomic_DNA.
DR PIR; JU0096; SXBPT4.
DR RefSeq; NP_049811.1; NC_000866.4.
DR GeneID; 1258760; -.
DR KEGG; vg:1258760; -.
DR BRENDA; 2.4.2.30; 732.
DR Proteomes; UP000009087; Genome.
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; IDA:UniProtKB.
DR GO; GO:0018120; P:peptidyl-arginine ADP-ribosylation; IMP:CACAO.
DR GO; GO:0006471; P:protein ADP-ribosylation; IDA:CACAO.
DR GO; GO:0046782; P:regulation of viral transcription; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Glycosyltransferase; NAD; Nucleotidyltransferase; Reference proteome;
KW Transferase; Virion.
FT PROPEP 1..6
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04139,
FT ECO:0000269|PubMed:8053153"
FT /id="PRO_0000003322"
FT CHAIN 7..682
FT /note="NAD(+)--arginine ADP-ribosyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04139"
FT /id="PRO_0000003323"
FT DOMAIN 383..614
FT /note="TR mART core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 478
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 503
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 576
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT SITE 6..7
FT /note="Cleavage"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04139,
FT ECO:0000269|PubMed:8053153"
FT CONFLICT 22..38
FT /note="KKKIPQIFSVHVDDAIE -> RRKYRKFFQFMLMMQLN (in Ref. 1;
FT CAA33807)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="A -> G (in Ref. 1; CAA33807)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="K -> R (in Ref. 1; CAA33807)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="T -> LQ (in Ref. 1; CAA33807)"
FT /evidence="ECO:0000305"
FT CONFLICT 658..661
FT /note="KVES -> ESRNR (in Ref. 1; CAA33807)"
FT /evidence="ECO:0000305"
FT CONFLICT 665..669
FT /note="IIASC -> NYLRLA (in Ref. 1; CAA33807)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 682 AA; 75818 MW; DE31BDC56AE4C427 CRC64;
MELITELFDE DTTLPITNLY PKKKIPQIFS VHVDDAIEQP GFRLCTYTSG GDTNRDLKMG
DKMMHIVPFT LTAKGSIAKL KGLGPSPINY INSVFTVAMQ TMRQYKIDAC MLRILKSKTA
GQARQIQVIA DRLIRSRSGG RYVLLKELWD YDKKYAYILI HRKNVSLEDI PGVPEISTEL
FTKVESKVGD VYINKDTGAQ VTKNEAIAAS IAQENDKRSD QAVIVKVKIS RRAIAQSQSL
ESSRFETPMF QKFEASAAEL NKPADAPLIS DSNELTVIST SGFALENALS SVTAGMAFRE
ASIIPEDKES IINAEIKNKA LERLRKESIT SIKTLETIAS IVDDTLEKYK GAWFERNINK
HSHLNQDAAN ELVQNSWNAI KTKIIRRELR GYALTAGWSL HPIVENKDSS KYTPAQKRGI
REYVGSGYVD INNALLGLYN PDERTSILTA SDIEKAIDNL DSAFKNGERL PKGITLYRSQ
RMLPSIYEAM VKNRVFYFRN FVSTSLYPNI FGTWMTDSSI GVLPDEKRLS VSIDKTDEGL
VNSSDNLVGI GWVITGADKV NVVLPGGSLA PSNEMEVILP RGLMVKVNKI TDASYNDGTV
KTNNKLIQAE VMTTEELTES VIYDGDHLME TGELVTMTGD IEDRVDFASF VSSNVKQKVE
SSLGIIASCI DIANMPYKFV QG
