NLEB2_ECOLR
ID NLEB2_ECOLR Reviewed; 326 AA.
AC A0A023YYV9;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Protein-arginine N-acetylglucosaminyltransferase NleB2 {ECO:0000305};
DE Short=Arginine GlcNAcyltransferase NleB2 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000250|UniProtKB:B7UNX3};
GN Name=nleB2 {ECO:0000303|PubMed:30327479};
GN ORFNames=ECRM12581_12505 {ECO:0000312|EMBL:AHY71031.1};
OS Escherichia coli O145:H28 (strain RM12581).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=1248823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM12581;
RX PubMed=24855308; DOI=10.1128/genomea.00482-14;
RA Cooper K.K., Mandrell R.E., Louie J.W., Korlach J., Clark T.A.,
RA Parker C.T., Huynh S., Chain P.S., Ahmed S., Carter M.Q.;
RT "Complete Genome Sequences of Two Escherichia coli O145:H28 Outbreak
RT Strains of Food Origin.";
RL Genome Announc. 2:e00482-e00482(2014).
RN [2] {ECO:0007744|PDB:5H5Y}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF MUTANT SER-21/SER-199, AND
RP MUTAGENESIS OF CYS-21 AND CYS-199.
RX PubMed=30327479; DOI=10.1038/s41467-018-06680-6;
RA Park J.B., Kim Y.H., Yoo Y., Kim J., Jun S.H., Cho J.W., El Qaidi S.,
RA Walpole S., Monaco S., Garcia-Garcia A.A., Wu M., Hays M.P.,
RA Hurtado-Guerrero R., Angulo J., Hardwidge P.R., Shin J.S., Cho H.S.;
RT "Structural basis for arginine glycosylation of host substrates by
RT bacterial effector proteins.";
RL Nat. Commun. 9:4283-4283(2018).
CC -!- FUNCTION: Protein-arginine N-acetylglucosaminyltransferase effector
CC that catalyzes the transfer of a single N-acetylglucosamine (GlcNAc) to
CC a conserved arginine residue of host target proteins. In contrast to
CC NleB1, not able to disrupt TNF signaling in infected cells. Shows a
CC lower enzymatic activity than NleB1. {ECO:0000250|UniProtKB:B7UNX3}.
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:B7UNX3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66633;
CC Evidence={ECO:0000250|UniProtKB:B7UNX3};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:B7UI21};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A0A482PDI9}. Host
CC cell {ECO:0000250|UniProtKB:A0A482PDI9}. 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:0000250|UniProtKB:B7UI21}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase NleB family.
CC {ECO:0000305}.
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DR EMBL; CP007136; AHY71031.1; -; Genomic_DNA.
DR RefSeq; WP_022581903.1; NZ_CP007136.1.
DR PDB; 5H5Y; X-ray; 2.30 A; A/B=1-326.
DR PDB; 6AI4; X-ray; 2.10 A; A/B=1-326.
DR PDBsum; 5H5Y; -.
DR PDBsum; 6AI4; -.
DR AlphaFoldDB; A0A023YYV9; -.
DR SMR; A0A023YYV9; -.
DR EnsemblBacteria; AHY71031; AHY71031; ECRM12581_12505.
DR PATRIC; fig|1248823.7.peg.2570; -.
DR HOGENOM; CLU_081850_0_0_6; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043657; C:host cell; 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 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Manganese; Metal-binding; Secreted;
KW Toxin; Transferase; Virulence.
FT CHAIN 1..326
FT /note="Protein-arginine N-acetylglucosaminyltransferase
FT NleB2"
FT /id="PRO_0000452595"
FT MOTIF 218..220
FT /note="DXD motif"
FT /evidence="ECO:0000305"
FT ACT_SITE 250
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:B7UI21"
FT BINDING 45..47
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:B7UI21"
FT BINDING 69
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:B7UI21"
FT BINDING 216..219
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:B7UI21"
FT BINDING 220
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B7UI21"
FT BINDING 317
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B7UI21"
FT BINDING 319
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:B7UI21"
FT BINDING 319
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:B7UI21"
FT BINDING 324..326
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:B7UI21"
FT MUTAGEN 21
FT /note="C->S: Mutant used for crystallization; prevents
FT protein precipitation due to irregular intermolecular
FT disulfide bonds; when associated with S-199."
FT /evidence="ECO:0000269|PubMed:30327479"
FT MUTAGEN 199
FT /note="C->S: Mutant used for crystallization; prevents
FT protein precipitation due to irregular intermolecular
FT disulfide bonds; when associated with S-21."
FT /evidence="ECO:0000269|PubMed:30327479"
SQ SEQUENCE 326 AA; 38010 MW; 33617962170A59AB CRC64;
MLSPIRTTFH NSVNIVQSSP CQTVSFAGKE YELKVIDEKT PILFQWFEPN PERYKKDEVP
IVNTKQHPYL DNVTNAARIE SDRMIGIFVD GDFSVNQKTA FSKLERDFEN VMIIYREDVD
FSMYDRKLSD IYHDIICEQR LRTEDKRDEY LLNLLEKELR EISKAQDSLI SMYAKKRNHA
WFDFFRNLAL LKAGEIFRCT YNTKNHGISF GEGGIYLDMD MILTGKLGTI YAPDGISMHV
DRRNDSVNIE NSAIIVNRSN HPALLEGLSF MHSKVDAHPY YDGLGKGVKK YFNFTPLHNY
NHFCDFIEFN HPNIIMNTSQ YTCSSW
