SSEK2_SALTY
ID SSEK2_SALTY Reviewed; 348 AA.
AC Q8ZNP4;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Protein-arginine N-acetylglucosaminyltransferase SseK2 {ECO:0000305};
DE Short=Arginine GlcNAcyltransferase SseK2 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000250|UniProtKB:P0DUJ8};
DE AltName: Full=Salmonella secreted effector K2 {ECO:0000303|PubMed:15322005};
GN Name=sseK2 {ECO:0000303|PubMed:15322005};
GN OrderedLocusNames=STM2137 {ECO:0000312|EMBL:AAL21040.1};
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP SUBCELLULAR LOCATION.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=15322005; DOI=10.1128/iai.72.9.5115-5125.2004;
RA Kujat Choy S.L., Boyle E.C., Gal-Mor O., Goode D.L., Valdez Y.,
RA Vallance B.A., Finlay B.B.;
RT "SseK1 and SseK2 are novel translocated proteins of Salmonella enterica
RT serovar typhimurium.";
RL Infect. Immun. 72:5115-5125(2004).
RN [3]
RP FUNCTION.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
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 [4]
RP ACTIVITY REGULATION.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=30619781; DOI=10.3389/fcimb.2018.00435;
RA El Qaidi S., Zhu C., McDonald P., Roy A., Maity P.K., Rane D., Perera C.,
RA Hardwidge P.R.;
RT "High-throughput screening for bacterial glycosyltransferase inhibitors.";
RL Front. Cell. Infect. Microbiol. 8:435-435(2018).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 14028 / SGSC 2980 / CDC 6516-60 / NCTC 12023;
RX PubMed=28069818; DOI=10.1128/iai.00010-17;
RA Guenster R.A., Matthews S.A., Holden D.W., Thurston T.L.M.;
RT "SseK1 and SseK3 type III secretion system effectors inhibit NF-kappaB
RT signaling and necroptotic cell death in salmonella-infected macrophages.";
RL Infect. Immun. 85:0-0(2017).
CC -!- FUNCTION: Protein-arginine N-acetylglucosaminyltransferase effector
CC that catalyzes the transfer of a single N-acetylglucosamine (GlcNAc) to
CC a conserved arginine residue in the death domain of host proteins such
CC as FADD: arginine GlcNAcylation prevents homotypic/heterotypic death
CC domain interactions (PubMed:28522607). Also acts on host proteins
CC without a death domain: catalyzes arginine GlcNAcylation of host small
CC Rab1 GTPase, thereby preventing GTPase activity and leading to impaired
CC host vesicular protein transport (By similarity). In contrast to Ssek1,
CC not able to disrupt TNF signaling in infected cells (PubMed:28522607).
CC {ECO:0000250|UniProtKB:P0DUJ8, ECO:0000269|PubMed:28522607}.
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:P0DUJ8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66633;
CC Evidence={ECO:0000250|UniProtKB:P0DUJ8};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P0DUJ8};
CC -!- ACTIVITY REGULATION: Protein-arginine N-acetylglucosaminyltransferase
CC activity is inhibited by 100066N compound (flavone analog) and 102644N
CC compound (a substituted isoxazole). {ECO:0000269|PubMed:30619781}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15322005}. Host
CC Golgi apparatus {ECO:0000269|PubMed:28069818}. Note=Secreted via the
CC type III secretion system (TTSS). {ECO:0000269|PubMed:15322005}.
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:P0DUJ8}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase NleB family.
CC {ECO:0000305}.
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DR EMBL; AE006468; AAL21040.1; -; Genomic_DNA.
DR RefSeq; NP_461081.1; NC_003197.2.
DR RefSeq; WP_010989041.1; NC_003197.2.
DR AlphaFoldDB; Q8ZNP4; -.
DR SMR; Q8ZNP4; -.
DR PaxDb; Q8ZNP4; -.
DR EnsemblBacteria; AAL21040; AAL21040; STM2137.
DR GeneID; 1253658; -.
DR KEGG; stm:STM2137; -.
DR PATRIC; fig|99287.12.peg.2261; -.
DR HOGENOM; CLU_081850_0_0_6; -.
DR OMA; LHNYNAF; -.
DR PhylomeDB; Q8ZNP4; -.
DR BioCyc; SENT99287:STM2137-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043657; C:host cell; IDA:UniProtKB.
DR GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106362; F:protein-arginine N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Glycosyltransferase; Host Golgi apparatus; Manganese; Metal-binding;
KW Reference proteome; Secreted; Toxin; Transferase; Virulence.
FT CHAIN 1..348
FT /note="Protein-arginine N-acetylglucosaminyltransferase
FT SseK2"
FT /id="PRO_0000452599"
FT MOTIF 239..241
FT /note="DXD motif"
FT /evidence="ECO:0000305"
FT ACT_SITE 271
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0DUJ8"
FT BINDING 64..66
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:P0DUJ8"
FT BINDING 88
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:P0DUJ8"
FT BINDING 237..240
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:P0DUJ8"
FT BINDING 241
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P0DUJ8"
FT BINDING 338
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P0DUJ8"
FT BINDING 338
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:P0DUJ8"
FT BINDING 340
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P0DUJ8"
FT BINDING 340
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:P0DUJ8"
FT BINDING 345..348
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:P0DUJ8"
SQ SEQUENCE 348 AA; 39566 MW; 4870E64CD4055C8E CRC64;
MARFNAAFTR IKIMFSRIRG LISCQSNTQT IAPTLSPPSS GHVSFAGIDY PLLPLNHQTP
LVFQWFERNP DRFGQNEIPI INTQKNPYLN NIINAAIIEK ERIIGIFVDG DFSKGQRKAL
GKLEQNYRNI KVIYNSDLNY SMYDKKLTTI YLENITKLEA QSASERDEVL LNGVKKSLED
VLKNNPEETL ISSHNKDKGH LWFDFYRNLF LLKGSDAFLE AGKPGCHHLQ PGGGCIYLDA
DMLLTDKLGT LYLPDGIAIH VSRKDNHVSL ENGIIAVNRS EHPALIKGLE IMHSKPYGDP
YNDWLSKGLR HYFDGSHIQD YDAFCDFIEF KHENIIMNTS SLTASSWR
