GSTA_BPT4
ID GSTA_BPT4 Reviewed; 400 AA.
AC P04519;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=DNA alpha-glucosyltransferase;
DE Short=AGT;
DE Short=Alpha-GT;
DE EC=2.4.1.26 {ECO:0000269|PubMed:6078540};
GN Name=agt;
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=4018026; DOI=10.1002/j.1460-2075.1985.tb02344.x;
RA Gram H., Rueger W.;
RT "Genes 55, alpha gt, 47 and 46 of bacteriophage T4: the genomic
RT organization as deduced by sequence analysis.";
RL EMBO J. 4:257-264(1985).
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 CATALYTIC ACTIVITY.
RX PubMed=6078540; DOI=10.1111/j.1432-1033.1967.tb00139.x;
RA de Waard A., Ubbink T.E., Beukman W.;
RT "On the specificity of bacteriophage-induced hydroxymethylcytosine
RT glucosyltransferases. II. Specificities of hydroxymethylcytosine alphaand
RT beta-glucosyltransferases induced by bacteriophage T4.";
RL Eur. J. Biochem. 2:303-308(1967).
RN [4]
RP FUNCTION, AND INTERACTION WITH GP45.
RX PubMed=15381072; DOI=10.1016/j.bbrc.2004.08.170;
RA Sommer N., Depping R., Piotrowski M., Ruger W.;
RT "Bacteriophage T4 alpha-glucosyltransferase: a novel interaction with gp45
RT and aspects of the catalytic mechanism.";
RL Biochem. Biophys. Res. Commun. 323:809-815(2004).
RN [5]
RP FUNCTION.
RX PubMed=26081634; DOI=10.1128/mbio.00648-15;
RA Bryson A.L., Hwang Y., Sherrill-Mix S., Wu G.D., Lewis J.D., Black L.,
RA Clark T.A., Bushman F.D.;
RT "Covalent Modification of Bacteriophage T4 DNA Inhibits CRISPR-Cas9.";
RL MBio 6:E00648-E00648(2015).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) IN COMPLEX WITH SUBSTRATES.
RX PubMed=16081100; DOI=10.1016/j.jmb.2005.07.007;
RA Lariviere L., Sommer N., Morera S.;
RT "Structural evidence of a passive base-flipping mechanism for AGT, an
RT unusual GT-B glycosyltransferase.";
RL J. Mol. Biol. 352:139-150(2005).
CC -!- FUNCTION: Catalyzes the transfer of glucose from uridine
CC diphosphoglucose to 5-hydroxymethyl cytosine of T4 DNA to yield
CC glucosyl 5-hydroxymethyl cytosine (glc-HMC) (PubMed:15381072). This DNA
CC process seems to occur immediately after DNA synthesis since the DNA
CC alpha-glucosyltransferase interacts with the clamp protein gp45
CC (PubMed:15381072). The glc-HMC modification protects the phage genome
CC against its own nucleases and the host restriction endonuclease system
CC (PubMed:15381072). The glc-HMC modification also protects against the
CC host CRISPR-Cas9 defense system (PubMed:26081634).
CC {ECO:0000269|PubMed:15381072, ECO:0000269|PubMed:26081634}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Transfers an alpha-D-glucosyl residue from UDP-glucose to a
CC hydroxymethylcytosine residue in DNA.; EC=2.4.1.26;
CC Evidence={ECO:0000269|PubMed:6078540};
CC -!- PATHWAY: Genetic information processing; DNA modification.
CC -!- SUBUNIT: Interacts with clamp protein gp45.
CC {ECO:0000269|PubMed:15381072, ECO:0000269|PubMed:16081100}.
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DR EMBL; X01804; CAA25940.1; -; Genomic_DNA.
DR EMBL; M10160; AAC05390.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42527.1; -; Genomic_DNA.
DR PIR; A00577; XUBPA4.
DR RefSeq; NP_049673.1; NC_000866.4.
DR PDB; 1XV5; X-ray; 1.73 A; A=1-400.
DR PDB; 1Y6F; X-ray; 2.40 A; A/B=1-400.
DR PDB; 1Y6G; X-ray; 2.80 A; A/B=1-400.
DR PDB; 1Y8Z; X-ray; 1.90 A; A/B=1-400.
DR PDB; 1YA6; X-ray; 2.40 A; A/B=1-400.
DR PDBsum; 1XV5; -.
DR PDBsum; 1Y6F; -.
DR PDBsum; 1Y6G; -.
DR PDBsum; 1Y8Z; -.
DR PDBsum; 1YA6; -.
DR SMR; P04519; -.
DR CAZy; GT72; Glycosyltransferase Family 72.
DR PRIDE; P04519; -.
DR GeneID; 1258823; -.
DR KEGG; vg:1258823; -.
DR UniPathway; UPA00198; -.
DR EvolutionaryTrace; P04519; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0033820; F:DNA alpha-glucosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006304; P:DNA modification; IEA:UniProtKB-UniPathway.
DR GO; GO:0099018; P:evasion by virus of host restriction-modification system; IEA:UniProtKB-KW.
DR GO; GO:0098672; P:inhibition of host CRISPR-cas system by virus; IEA:UniProtKB-KW.
DR InterPro; IPR016223; DNA_alpha-glucosyltransferase.
DR Pfam; PF11440; AGT; 1.
DR PIRSF; PIRSF000471; DNA_alpha-glucosyltransferase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; CRISPR-cas system evasion by virus; Glycosyltransferase;
KW Host-virus interaction; Reference proteome;
KW Restriction-modification system evasion by virus; Transferase.
FT CHAIN 1..400
FT /note="DNA alpha-glucosyltransferase"
FT /id="PRO_0000164941"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1XV5"
FT HELIX 15..29
FT /evidence="ECO:0007829|PDB:1XV5"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:1XV5"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:1XV5"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1XV5"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1XV5"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1XV5"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1XV5"
FT HELIX 65..72
FT /evidence="ECO:0007829|PDB:1XV5"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:1XV5"
FT HELIX 90..102
FT /evidence="ECO:0007829|PDB:1XV5"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:1XV5"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:1XV5"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1XV5"
FT HELIX 127..133
FT /evidence="ECO:0007829|PDB:1XV5"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:1XV5"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1YA6"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:1XV5"
FT HELIX 150..154
FT /evidence="ECO:0007829|PDB:1XV5"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1XV5"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1XV5"
FT HELIX 180..187
FT /evidence="ECO:0007829|PDB:1XV5"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:1XV5"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:1XV5"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:1XV5"
FT HELIX 211..220
FT /evidence="ECO:0007829|PDB:1XV5"
FT TURN 221..226
FT /evidence="ECO:0007829|PDB:1XV5"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:1XV5"
FT HELIX 238..245
FT /evidence="ECO:0007829|PDB:1XV5"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:1XV5"
FT HELIX 255..260
FT /evidence="ECO:0007829|PDB:1XV5"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:1XV5"
FT STRAND 269..273
FT /evidence="ECO:0007829|PDB:1XV5"
FT HELIX 277..285
FT /evidence="ECO:0007829|PDB:1XV5"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:1XV5"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:1XV5"
FT HELIX 307..315
FT /evidence="ECO:0007829|PDB:1XV5"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:1XV5"
FT HELIX 323..328
FT /evidence="ECO:0007829|PDB:1XV5"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:1XV5"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:1XV5"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:1XV5"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:1Y8Z"
FT HELIX 353..364
FT /evidence="ECO:0007829|PDB:1XV5"
FT HELIX 367..385
FT /evidence="ECO:0007829|PDB:1XV5"
FT HELIX 387..398
FT /evidence="ECO:0007829|PDB:1XV5"
SQ SEQUENCE 400 AA; 46704 MW; 09CC1D4800F5AD2E CRC64;
MRICIFMARG LEGCGVTKFS LEQRDWFIKN GHEVTLVYAK DKSFTRTSSH DHKSFSIPVI
LAKEYDKALK LVNDCDILII NSVPATSVQE ATINNYKKLL DNIKPSIRVV VYQHDHSVLS
LRRNLGLEET VRRADVIFSH SDNGDFNKVL MKEWYPETVS LFDDIEEAPT VYNFQPPMDI
VKVRSTYWKD VSEINMNINR WIGRTTTWKG FYQMFDFHEK FLKPAGKSTV MEGLERSPAF
IAIKEKGIPY EYYGNREIDK MNLAPNQPAQ ILDCYINSEM LERMSKSGFG YQLSKLNQKY
LQRSLEYTHL ELGACGTIPV FWKSTGENLK FRVDNTPLTS HDSGIIWFDE NDMESTFERI
KELSSDRALY DREREKAYEF LYQHQDSSFC FKEQFDIITK
