NLEB1_ECO27
ID NLEB1_ECO27 Reviewed; 329 AA.
AC B7UI21;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Protein-arginine N-acetylglucosaminyltransferase NleB1 {ECO:0000305};
DE Short=Arginine GlcNAcyltransferase NleB1 {ECO:0000303|PubMed:30979585};
DE EC=2.4.1.- {ECO:0000269|PubMed:23955153, ECO:0000269|PubMed:24025841, ECO:0000269|PubMed:26883593, ECO:0000269|PubMed:28860194, ECO:0000269|PubMed:30125331, ECO:0000269|PubMed:30979585, ECO:0000269|PubMed:32432056};
DE AltName: Full=Non-LEE-encoded type III effector B1 {ECO:0000303|PubMed:20485572};
GN Name=nleB1 {ECO:0000303|PubMed:20485572};
GN Synonyms=nleB {ECO:0000303|PubMed:28860194, ECO:0000303|PubMed:32432056};
GN OrderedLocusNames=E2348C_3231 {ECO:0000312|EMBL:CAS10779.1};
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC;
RX PubMed=18952797; DOI=10.1128/jb.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(2009).
RN [2]
RP FUNCTION.
RC STRAIN=E2348/69 / EPEC;
RX PubMed=20126447; DOI=10.1371/journal.ppat.1000743;
RA Nadler C., Baruch K., Kobi S., Mills E., Haviv G., Farago M., Alkalay I.,
RA Bartfeld S., Meyer T.F., Ben-Neriah Y., Rosenshine I.;
RT "The type III secretion effector NleE inhibits NF-kappaB activation.";
RL PLoS Pathog. 6:e1000743-e1000743(2010).
RN [3]
RP FUNCTION.
RC STRAIN=E2348/69 / EPEC;
RX PubMed=20485572; DOI=10.1371/journal.ppat.1000898;
RA Newton H.J., Pearson J.S., Badea L., Kelly M., Lucas M., Holloway G.,
RA Wagstaff K.M., Dunstone M.A., Sloan J., Whisstock J.C., Kaper J.B.,
RA Robins-Browne R.M., Jans D.A., Frankel G., Phillips A.D., Coulson B.S.,
RA Hartland E.L.;
RT "The type III effectors NleE and NleB from enteropathogenic E. coli and
RT OspZ from Shigella block nuclear translocation of NF-kappaB p65.";
RL PLoS Pathog. 6:e1000898-e1000898(2010).
RN [4]
RP FUNCTION.
RC STRAIN=E2348/69 / EPEC;
RX PubMed=22144899; DOI=10.1371/journal.ppat.1002414;
RA Ruchaud-Sparagano M.H., Muehlen S., Dean P., Kenny B.;
RT "The enteropathogenic E. coli (EPEC) Tir effector inhibits NF-kappaB
RT activity by targeting TNFalpha receptor-associated factors.";
RL PLoS Pathog. 7:e1002414-e1002414(2011).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF
RP 221-ASP--ASP-223.
RC STRAIN=E2348/69 / EPEC;
RX PubMed=23955153; DOI=10.1038/nature12436;
RA Li S., Zhang L., Yao Q., Li L., Dong N., Rong J., Gao W., Ding X., Sun L.,
RA Chen X., Chen S., Shao F.;
RT "Pathogen blocks host death receptor signalling by arginine GlcNAcylation
RT of death domains.";
RL Nature 501:242-246(2013).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF
RP 221-ASP--ASP-223.
RC STRAIN=E2348/69 / EPEC;
RX PubMed=24025841; DOI=10.1038/nature12524;
RA Pearson J.S., Giogha C., Ong S.Y., Kennedy C.L., Kelly M., Robinson K.S.,
RA Lung T.W., Mansell A., Riedmaier P., Oates C.V., Zaid A., Muehlen S.,
RA Crepin V.F., Marches O., Ang C.S., Williamson N.A., O'Reilly L.A.,
RA Bankovacki A., Nachbur U., Infusini G., Webb A.I., Silke J., Strasser A.,
RA Frankel G., Hartland E.L.;
RT "A type III effector antagonizes death receptor signalling during bacterial
RT gut infection.";
RL Nature 501:247-251(2013).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 63-PRO--ASN-66; TYR-219;
RP 221-ASP--ASP-223; 236-PRO--GLY-238 AND GLU-253.
RC STRAIN=E2348/69 / EPEC;
RX PubMed=26883593; DOI=10.1128/iai.01523-15;
RA Wong Fok Lung T., Giogha C., Creuzburg K., Ong S.Y., Pollock G.L.,
RA Zhang Y., Fung K.Y., Pearson J.S., Hartland E.L.;
RT "Mutagenesis and functional analysis of the bacterial arginine
RT glycosyltransferase effector NleB1 from enteropathogenic Escherichia
RT coli.";
RL Infect. Immun. 84:1346-1360(2016).
RN [8]
RP FUNCTION.
RC STRAIN=E2348/69 / EPEC;
RX PubMed=28138023; DOI=10.1128/iai.01071-16;
RA Pollock G.L., Oates C.V.L., Giogha C., Wong Fok Lung T., Ong S.Y.,
RA Pearson J.S., Hartland E.L.;
RT "Distinct Roles of the antiapoptotic effectors NleB and NleF from
RT enteropathogenic Escherichia coli.";
RL Infect. Immun. 85:0-0(2017).
RN [9]
RP FUNCTION.
RC STRAIN=E2348/69 / EPEC;
RX PubMed=28522607; DOI=10.1074/jbc.m117.790675;
RA El Qaidi S., Chen K., Halim A., Siukstaite L., Rueter C.,
RA Hurtado-Guerrero R., Clausen H., Hardwidge P.R.;
RT "NleB/SseK effectors from Citrobacter rodentium, Escherichia coli, and
RT Salmonella enterica display distinct differences in host substrate
RT specificity.";
RL J. Biol. Chem. 292:11423-11430(2017).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 221-ASP--ASP-223.
RC STRAIN=E2348/69 / EPEC;
RX PubMed=28860194; DOI=10.1074/jbc.m117.805036;
RA Scott N.E., Giogha C., Pollock G.L., Kennedy C.L., Webb A.I.,
RA Williamson N.A., Pearson J.S., Hartland E.L.;
RT "The bacterial arginine glycosyltransferase effector NleB preferentially
RT modifies Fas-associated death domain protein (FADD).";
RL J. Biol. Chem. 292:17337-17350(2017).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 221-ASP--ASP-223.
RC STRAIN=E2348/69 / EPEC;
RX PubMed=30125331; DOI=10.1371/journal.ppat.1007259;
RA Xu C., Liu X., Zha H., Fan S., Zhang D., Li S., Xiao W.;
RT "A pathogen-derived effector modulates host glucose metabolism by arginine
RT GlcNAcylation of HIF-1alpha protein.";
RL PLoS Pathog. 14:e1007259-e1007259(2018).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AUTOGLYCOSYLATION,
RP GLYCOSYLATION AT ARG-13; ARG-53; ARG-159 AND ARG-293, AND MUTAGENESIS OF
RP ARG-13; ARG-53; ARG-159 AND ARG-293.
RC STRAIN=E2348/69 / EPEC;
RX PubMed=32432056; DOI=10.3389/fcimb.2020.00197;
RA Xue J., Pan X., Peng T., Duan M., Du L., Zhuang X., Cai X., Yi X., Fu Y.,
RA Li S.;
RT "Auto arginine-GlcNAcylation is crucial for bacterial pathogens in
RT regulating host cell death.";
RL Front. Cell. Infect. Microbiol. 10:197-197(2020).
RN [13]
RP FUNCTION.
RX PubMed=31974499; DOI=10.1038/s41598-020-58062-y;
RA El Qaidi S., Scott N.E., Hays M.P., Geisbrecht B.V., Watkins S.,
RA Hardwidge P.R.;
RT "An intra-bacterial activity for a T3SS effector.";
RL Sci. Rep. 10:1073-1073(2020).
RN [14] {ECO:0007744|PDB:6ACI, ECO:0007744|PDB:6E66}
RP X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 28-329 IN COMPLEX WITH
RP URIDINE-5'-DIPHOSPHATE; MANGANESE AND HOST FADD, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, ACTIVE SITE, DOMAIN, AND MUTAGENESIS OF TRP-49; GLU-58;
RP TYR-145; ASP-151; PHE-185; ASP-186; ARG-189; TYR-219; ASP-221; ASP-223;
RP GLU-253; 277-LYS--ASP-279; LYS-277; TYR-283; 284-TYR-ASP-285 AND
RP 289-LYS--LYS-292.
RX PubMed=30979585; DOI=10.1016/j.molcel.2019.03.028;
RA Ding J., Pan X., Du L., Yao Q., Xue J., Yao H., Wang D.C., Li S., Shao F.;
RT "Structural and functional insights into host death domains inactivation by
RT the bacterial arginine GlcNAcyltransferase effector.";
RL Mol. Cell 74:922-935(2019).
CC -!- FUNCTION: Protein-arginine N-acetylglucosaminyltransferase effector
CC that disrupts TNF signaling in infected cells, including NF-kappa-B
CC signaling, apoptosis and necroptosis (PubMed:20126447, PubMed:20485572,
CC PubMed:22144899, PubMed:23955153, PubMed:24025841, PubMed:28138023,
CC PubMed:28522607, PubMed:30979585). Acts by catalyzing the transfer of a
CC single N-acetylglucosamine (GlcNAc) to a conserved arginine residue in
CC the death domain of host proteins FADD, TRADD, FAS, TNFRSF1A/TNFR1,
CC TNFRSF25/DR3 and RIPK1: arginine GlcNAcylation prevents
CC homotypic/heterotypic death domain interactions and assembly of the
CC oligomeric TNF-alpha receptor complex, thereby disrupting TNF signaling
CC (PubMed:23955153, PubMed:24025841, PubMed:26883593, PubMed:28522607,
CC PubMed:28860194, PubMed:30979585). Has preference for host FADD as
CC substrate compared to other death domain-containing proteins
CC (PubMed:28860194). Also acts on host proteins without a death domain:
CC catalyzes arginine GlcNAcylation of HIF1A, thereby regulating host
CC glucose metabolism (PubMed:30125331). Also displays intra-bacterial
CC activity by mediating GlcNAcylation of glutathione synthetase GshB
CC (PubMed:31974499). Catalyzes auto-GlcNAcylation, which is required for
CC activity toward death domain-containing host target proteins
CC (PubMed:32432056). Shows a higher enzymatic activity than NleB2
CC (PubMed:23955153). {ECO:0000269|PubMed:20126447,
CC ECO:0000269|PubMed:20485572, ECO:0000269|PubMed:22144899,
CC ECO:0000269|PubMed:23955153, ECO:0000269|PubMed:24025841,
CC ECO:0000269|PubMed:26883593, ECO:0000269|PubMed:28138023,
CC ECO:0000269|PubMed:28522607, ECO:0000269|PubMed:28860194,
CC ECO:0000269|PubMed:30125331, ECO:0000269|PubMed:30979585,
CC ECO:0000269|PubMed:31974499, ECO:0000269|PubMed:32432056}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+)
CC + N(omega)-(N-acetyl-beta-D-glucosaminyl)-L-arginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:66632, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:17079,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:167322;
CC Evidence={ECO:0000269|PubMed:23955153, ECO:0000269|PubMed:24025841,
CC ECO:0000269|PubMed:26883593, ECO:0000269|PubMed:28860194,
CC ECO:0000269|PubMed:30125331, ECO:0000269|PubMed:30979585,
CC ECO:0000269|PubMed:32432056};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66633;
CC Evidence={ECO:0000269|PubMed:23955153, ECO:0000269|PubMed:24025841,
CC ECO:0000269|PubMed:26883593, ECO:0000269|PubMed:28860194,
CC ECO:0000269|PubMed:30125331, ECO:0000269|PubMed:30979585,
CC ECO:0000269|PubMed:32432056};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:23955153, ECO:0000269|PubMed:24025841,
CC ECO:0000269|PubMed:30979585};
CC -!- INTERACTION:
CC B7UI21; Q13158: FADD; Xeno; NbExp=7; IntAct=EBI-16070376, EBI-494804;
CC B7UI21; Q13546: RIPK1; Xeno; NbExp=4; IntAct=EBI-16070376, EBI-358507;
CC B7UI21; Q15628: TRADD; Xeno; NbExp=7; IntAct=EBI-16070376, EBI-359215;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A0A482PDI9}. Host
CC cytoplasm {ECO:0000269|PubMed:32432056}. Note=Secreted via the type III
CC secretion system (TTSS). {ECO:0000250|UniProtKB:A0A482PDI9}.
CC -!- DOMAIN: Adopts a GT-A fold and acts as an inverting enzyme that
CC converts the alpha-configuration in the UDP-N-acetyl-alpha-D-
CC glucosamine donor to the beta configuration in the N-linked (GlcNAc)
CC arginine product. {ECO:0000269|PubMed:30979585}.
CC -!- PTM: Auto-glycosylated: arginine GlcNAcylation is required for activity
CC toward death domain-containing host target proteins.
CC {ECO:0000269|PubMed:32432056}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase NleB family.
CC {ECO:0000305}.
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DR EMBL; FM180568; CAS10779.1; -; Genomic_DNA.
DR RefSeq; WP_012578998.1; NC_011601.1.
DR PDB; 6ACI; X-ray; 1.87 A; A=28-329.
DR PDB; 6E66; X-ray; 2.10 A; A=1-329.
DR PDBsum; 6ACI; -.
DR PDBsum; 6E66; -.
DR AlphaFoldDB; B7UI21; -.
DR SMR; B7UI21; -.
DR DIP; DIP-60511N; -.
DR IntAct; B7UI21; 3.
DR EnsemblBacteria; CAS10779; CAS10779; E2348C_3231.
DR KEGG; ecg:E2348C_3231; -.
DR HOGENOM; CLU_081850_0_0_6; -.
DR OMA; LHNYNAF; -.
DR Proteomes; UP000008205; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0106362; F:protein-arginine N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0034054; P:suppression by symbiont of host defense-related programmed cell death; IDA:UniProtKB.
DR GO; GO:0085034; P:suppression by symbiont of host I-kappaB kinase/NF-kappaB cascade; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Glycosyltransferase; Host cytoplasm; Manganese;
KW Metal-binding; Secreted; Toxin; Transferase; Virulence.
FT CHAIN 1..329
FT /note="Protein-arginine N-acetylglucosaminyltransferase
FT NleB1"
FT /id="PRO_0000452591"
FT MOTIF 221..223
FT /note="DXD motif"
FT /evidence="ECO:0000305"
FT ACT_SITE 253
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:30979585"
FT BINDING 48..50
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000305|PubMed:30979585,
FT ECO:0007744|PDB:6ACI"
FT BINDING 72
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000305|PubMed:30979585,
FT ECO:0007744|PDB:6ACI"
FT BINDING 219..222
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000305|PubMed:30979585,
FT ECO:0007744|PDB:6ACI"
FT BINDING 223
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:30979585,
FT ECO:0007744|PDB:6ACI"
FT BINDING 320
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:30979585,
FT ECO:0007744|PDB:6ACI"
FT BINDING 322
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:30979585,
FT ECO:0007744|PDB:6ACI"
FT BINDING 322
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000305|PubMed:30979585,
FT ECO:0007744|PDB:6ACI"
FT BINDING 327..329
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000305|PubMed:30979585,
FT ECO:0007744|PDB:6ACI"
FT CARBOHYD 13
FT /note="N-beta-linked (GlcNAc) arginine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:32432056"
FT CARBOHYD 53
FT /note="N-beta-linked (GlcNAc) arginine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:32432056"
FT CARBOHYD 159
FT /note="N-beta-linked (GlcNAc) arginine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:32432056"
FT CARBOHYD 293
FT /note="N-beta-linked (GlcNAc) arginine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:32432056"
FT MUTAGEN 13
FT /note="R->A: In 4RA; abolished auto-GlcNAcylation and
FT reduced activity toward death domain-containing host target
FT proteins; when associated with A-53, A-159 and A-293."
FT /evidence="ECO:0000269|PubMed:32432056"
FT MUTAGEN 49
FT /note="W->A: Abolished protein-arginine N-
FT acetylglucosaminyltransferase activity."
FT /evidence="ECO:0000269|PubMed:30979585"
FT MUTAGEN 53
FT /note="R->A: In 4RA; abolished auto-GlcNAcylation and
FT reduced activity toward death domain-containing host target
FT proteins; when associated with A-13, A-159 and A-293."
FT /evidence="ECO:0000269|PubMed:32432056"
FT MUTAGEN 58
FT /note="E->A: Does not affect ability to disrupt TNF
FT signaling in infected cells."
FT /evidence="ECO:0000269|PubMed:30979585"
FT MUTAGEN 63..66
FT /note="PILN->AAAA: Abolished protein-arginine N-
FT acetylglucosaminyltransferase activity. Does not affect
FT ability to interact with substrate host protein FADD."
FT /evidence="ECO:0000269|PubMed:26883593"
FT MUTAGEN 145
FT /note="Y->A: Strongly decreased protein-arginine N-
FT acetylglucosaminyltransferase activity; when associated
FT with A-151."
FT /evidence="ECO:0000269|PubMed:30979585"
FT MUTAGEN 151
FT /note="D->A: Strongly decreased protein-arginine N-
FT acetylglucosaminyltransferase activity; when associated
FT with A-145."
FT /evidence="ECO:0000269|PubMed:30979585"
FT MUTAGEN 159
FT /note="R->A: In 4RA; abolished auto-GlcNAcylation and
FT reduced activity toward death domain-containing host target
FT proteins; when associated with A-13, A-53 and A-293."
FT /evidence="ECO:0000269|PubMed:32432056"
FT MUTAGEN 185
FT /note="F->A: Does not affect protein-arginine N-
FT acetylglucosaminyltransferase activity."
FT /evidence="ECO:0000269|PubMed:30979585"
FT MUTAGEN 186
FT /note="D->A: Abolished protein-arginine N-
FT acetylglucosaminyltransferase activity."
FT /evidence="ECO:0000269|PubMed:30979585"
FT MUTAGEN 189
FT /note="R->A: Abolished protein-arginine N-
FT acetylglucosaminyltransferase activity."
FT /evidence="ECO:0000269|PubMed:30979585"
FT MUTAGEN 219
FT /note="Y->A: Abolished protein-arginine N-
FT acetylglucosaminyltransferase activity. Does not affect
FT ability to interact with substrate host protein FADD."
FT /evidence="ECO:0000269|PubMed:26883593,
FT ECO:0000269|PubMed:30979585"
FT MUTAGEN 221..223
FT /note="DAD->AAA: Abolished protein-arginine N-
FT acetylglucosaminyltransferase activity and ability to
FT disrupt TNF signaling in infected cells. Does not affect
FT ability to interact with substrate host protein FADD."
FT /evidence="ECO:0000269|PubMed:23955153,
FT ECO:0000269|PubMed:24025841, ECO:0000269|PubMed:26883593,
FT ECO:0000269|PubMed:28860194, ECO:0000269|PubMed:30125331"
FT MUTAGEN 221
FT /note="D->A: Abolished protein-arginine N-
FT acetylglucosaminyltransferase activity."
FT /evidence="ECO:0000269|PubMed:30979585"
FT MUTAGEN 223
FT /note="D->A: Abolished protein-arginine N-
FT acetylglucosaminyltransferase activity."
FT /evidence="ECO:0000269|PubMed:30979585"
FT MUTAGEN 236..238
FT /note="PDG->AAA: Abolished interaction with substrate host
FT protein FADD."
FT /evidence="ECO:0000269|PubMed:26883593"
FT MUTAGEN 253
FT /note="E->A: Abolished protein-arginine N-
FT acetylglucosaminyltransferase activity. Does not affect
FT ability to interact with substrate host protein FADD."
FT /evidence="ECO:0000269|PubMed:26883593,
FT ECO:0000269|PubMed:30979585"
FT MUTAGEN 277..279
FT /note="KVD->AVA: Abolished protein-arginine N-
FT acetylglucosaminyltransferase activity."
FT /evidence="ECO:0000269|PubMed:30979585"
FT MUTAGEN 277
FT /note="K->A: Abolished protein-arginine N-
FT acetylglucosaminyltransferase activity; when associated
FT with 289-A--A-292."
FT /evidence="ECO:0000269|PubMed:30979585"
FT MUTAGEN 283
FT /note="Y->A: Abolished protein-arginine N-
FT acetylglucosaminyltransferase activity."
FT /evidence="ECO:0000269|PubMed:30979585"
FT MUTAGEN 284..285
FT /note="YD->AA: Abolished protein-arginine N-
FT acetylglucosaminyltransferase activity."
FT /evidence="ECO:0000269|PubMed:30979585"
FT MUTAGEN 289..292
FT /note="KGIK->AGIA: Abolished protein-arginine N-
FT acetylglucosaminyltransferase activity; when associated
FT with A-277."
FT /evidence="ECO:0000269|PubMed:30979585"
FT MUTAGEN 293
FT /note="R->A: In 4RA; abolished auto-GlcNAcylation and
FT reduced activity toward death domain-containing host target
FT proteins; when associated with A-13, A-53 and A-159."
FT /evidence="ECO:0000269|PubMed:32432056"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:6ACI"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:6ACI"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:6ACI"
FT HELIX 72..82
FT /evidence="ECO:0007829|PDB:6ACI"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:6ACI"
FT HELIX 98..110
FT /evidence="ECO:0007829|PDB:6ACI"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:6ACI"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:6ACI"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:6ACI"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:6ACI"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:6ACI"
FT HELIX 152..163
FT /evidence="ECO:0007829|PDB:6ACI"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:6ACI"
FT HELIX 182..195
FT /evidence="ECO:0007829|PDB:6ACI"
FT HELIX 197..201
FT /evidence="ECO:0007829|PDB:6ACI"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:6ACI"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:6ACI"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:6ACI"
FT STRAND 239..246
FT /evidence="ECO:0007829|PDB:6ACI"
FT STRAND 249..261
FT /evidence="ECO:0007829|PDB:6ACI"
FT HELIX 265..274
FT /evidence="ECO:0007829|PDB:6ACI"
FT HELIX 282..287
FT /evidence="ECO:0007829|PDB:6ACI"
FT HELIX 288..294
FT /evidence="ECO:0007829|PDB:6ACI"
FT HELIX 303..310
FT /evidence="ECO:0007829|PDB:6ACI"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:6ACI"
SQ SEQUENCE 329 AA; 37627 MW; 77F71E1D309E1F39 CRC64;
MLSSLNVLQS SFRGKTALSN STLLQKVSFA GKEYSLEPID ERTPILFQWF EARPERYEKG
EVPILNTKEH PYLSNIINAA KIENERIIGV LVDGNFTYEQ KKEFLNLENE HQNIKIIYRA
DVDFSMYDKK LSDIYLENIH KQESYPASER DNYLLGLLRE ELKNIPEGKD SLIESYAEKR
EHTWFDFFRN LAILKAGSLF TETGKTGCHN ISPCSGCIYL DADMIITDKL GVLYAPDGIA
VHVDCNDEIK SLENGAIVVN RSNHPALLAG LDIMKSKVDA HPYYDGLGKG IKRHFNYSSL
HNYNAFCDFI EFKHENIIPN TSMYTSSSW
