SSEK1_SALE2
ID SSEK1_SALE2 Reviewed; 336 AA.
AC A0A656IJ15;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-JUN-2021, sequence version 2.
DT 03-AUG-2022, entry version 7.
DE RecName: Full=Protein-arginine N-acetylglucosaminyltransferase SseK1 {ECO:0000305};
DE Short=Arginine GlcNAcyltransferase SseK1 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q9L9J3};
DE AltName: Full=Salmonella secreted effector K1 {ECO:0000303|PubMed:29458091};
GN Name=sseK1 {ECO:0000303|PubMed:29458091};
GN ORFNames=A673_00934 {ECO:0000312|EMBL:EPI74832.1};
OS Salmonella enteritidis (strain 2009K0958).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1192586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2009K0958;
RA McClelland M., Porwollik S., Desai P., Cheng P., Wollam A., Pepin K.,
RA Palsikar V.B., Fulton L., Fulton R., Delehaunty K., Fronick C., Godfrey J.,
RA Waligorski J., Appelbaum E., Tomlinson C., Warren W., Sodergren E.,
RA Weinstock G., Wilson R.K.;
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13076 / CDC K-1891;
RX PubMed=29458091; DOI=10.1016/j.micpath.2018.02.030;
RA Yang Y., Yu C., Ding K., Zhang C., Liao C., Jia Y., Li J., Cheng X.;
RT "Role of the sseK1 gene in the pathogenicity of Salmonella enterica serovar
RT enteritidis in vitro and in vivo.";
RL Microb. Pathog. 117:270-275(2018).
CC -!- FUNCTION: Protein-arginine N-acetylglucosaminyltransferase effector
CC that disrupts TNF signaling in infected cells, including NF-kappa-B
CC signaling, apoptosis and necroptosis. Acts by catalyzing the transfer
CC of a single N-acetylglucosamine (GlcNAc) to a conserved arginine
CC residue in the death domain of host proteins TRADD and, to a lower
CC extent, FADD: arginine GlcNAcylation prevents homotypic/heterotypic
CC death domain interactions and assembly of the oligomeric TNF-alpha
CC receptor complex, thereby disrupting TNF signaling (By similarity).
CC Also acts on host proteins without a death domain: catalyzes arginine
CC GlcNAcylation of host GAPDH protein, thereby preventing GAPDH
CC interaction with TRAF2, leading to inhibit NF-kappa-B signaling (By
CC similarity). Catalyzes GlcNAcylation of host tubulin-folding cofactor
CC TBCB, thereby promoting microtubule stability (By similarity). Also
CC mediates auto-GlcNAcylation, which is required for activity toward
CC death domain-containing host target proteins (By similarity).
CC {ECO:0000250|UniProtKB:A0A0H3NK84, ECO:0000250|UniProtKB:Q9L9J3}.
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:0000250|UniProtKB:A0A0H3NK84};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66633;
CC Evidence={ECO:0000250|UniProtKB:A0A0H3NK84};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A0A0H3NK84};
CC -!- ACTIVITY REGULATION: Protein-arginine N-acetylglucosaminyltransferase
CC activity is inhibited by 100066N compound (flavone analog) and 102644N
CC compound (a substituted isoxazole). {ECO:0000250|UniProtKB:Q9L9J3}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9L9J3}. Host
CC cytoplasm, host cytosol {ECO:0000250|UniProtKB:A0A0H3NK84}.
CC Note=Secreted via type III secretion systems 1 and 2 (SPI-1 and SPI-2
CC TTSS). {ECO:0000250|UniProtKB:Q9L9J3}.
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:0000250|UniProtKB:A0A0H3NK84}.
CC -!- PTM: Auto-glycosylated: arginine GlcNAcylation is required for activity
CC toward death domain-containing host target proteins.
CC {ECO:0000250|UniProtKB:A0A0H3NK84}.
CC -!- DISRUPTION PHENOTYPE: Reduced virulence. {ECO:0000269|PubMed:29458091}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase NleB family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EPI74832.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; ATFT01000016; EPI74832.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000400600.1; NZ_KE349052.1.
DR AlphaFoldDB; A0A656IJ15; -.
DR SMR; A0A656IJ15; -.
DR Proteomes; UP000014535; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044164; C:host cell cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Glycoprotein; Glycosyltransferase; Host cytoplasm; Manganese;
KW Metal-binding; Secreted; Toxin; Transferase; Virulence.
FT CHAIN 1..336
FT /note="Protein-arginine N-acetylglucosaminyltransferase
FT SseK1"
FT /id="PRO_0000452598"
FT MOTIF 223..225
FT /note="DXD motif"
FT /evidence="ECO:0000305"
FT ACT_SITE 255
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3NK84"
FT BINDING 50..52
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3NK84"
FT BINDING 74
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3NK84"
FT BINDING 224..225
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3NK84"
FT BINDING 225
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3NK84"
FT BINDING 322
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3NK84"
FT BINDING 324
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3NK84"
FT BINDING 324
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3NK84"
FT BINDING 329
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3NK84"
FT CARBOHYD 24
FT /note="N-beta-linked (GlcNAc) arginine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3NK84"
FT CARBOHYD 152
FT /note="N-beta-linked (GlcNAc) arginine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3NK84"
FT CARBOHYD 333
FT /note="N-beta-linked (GlcNAc) arginine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:A0A0H3NK84"
SQ SEQUENCE 336 AA; 38836 MW; 77CB1A4B2316066F CRC64;
MIPPLNRYVP ALSKNELVKT VTNRDIQFTS FNGKDYPLCF LDEKTPLLFQ WFERNPARFG
KNDIPIINTE KNPYLNNIIK AATIEKERLI GIFVDGDFFP GQKDAFSKLE YDYENIKVIY
RNDIDFSMYD KKLSEIYMEN ISKQESMPEE KRDCHLLQLL KKELSDIQEG NDSLIKSYLL
DKGHGWFDFY RNMAMLKAGQ LFLEADKVGC YDLSTNSGCI YLDADMIITE KLGGIYIPDG
IAVHVERIDG RASMENGIIA VDRNNHPALL AGLEIMHTKF DADPYSDGVC NGIRKHFNYS
LNEDYNSFCD FIEFKHDNII MNTSQFTQSS WARHVQ
