NLEB2_ECO57
ID NLEB2_ECO57 Reviewed; 326 AA.
AC Q8X837; A0A0H3JCT5; A0A6M0JHG3; Q7AGE3;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
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:28522607};
GN ORFNames=ECs_0846 {ECO:0000312|EMBL:BAB34269.1};
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [2]
RP FUNCTION.
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
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).
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 (By similarity).
CC In contrast to NleB1, not able to disrupt TNF signaling in infected
CC cells (PubMed:28522607). Shows a lower enzymatic activity than NleB1
CC (By similarity). {ECO:0000250|UniProtKB:B7UNX3,
CC 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: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; BA000007; BAB34269.1; -; Genomic_DNA.
DR RefSeq; NP_308873.1; NC_002695.1.
DR RefSeq; WP_000950813.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8X837; -.
DR SMR; Q8X837; -.
DR STRING; 155864.EDL933_0890; -.
DR EnsemblBacteria; BAB34269; BAB34269; ECs_0846.
DR EnsemblBacteria; QCH83947; QCH83947; CAM50_0020190.
DR GeneID; 917585; -.
DR KEGG; ecs:ECs_0846; -.
DR PATRIC; fig|386585.9.peg.961; -.
DR eggNOG; ENOG502Z8RE; Bacteria.
DR HOGENOM; CLU_081850_0_0_6; -.
DR Proteomes; UP000000558; Chromosome.
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 3: Inferred from homology;
KW Glycosyltransferase; Manganese; Metal-binding; Reference proteome;
KW Secreted; Toxin; Transferase; Virulence.
FT CHAIN 1..326
FT /note="Protein-arginine N-acetylglucosaminyltransferase
FT NleB2"
FT /id="PRO_0000452594"
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"
SQ SEQUENCE 326 AA; 38056 MW; 807D0FB97ABC85DA CRC64;
MLSPIRTTFH NSVNIVQSSP CQTVSFAGKE YELKVIDEKT PILFQWFEPN PERYKKDEVP
IVNTKQHPYL DNVTNAARIE SDRMIGIFVD GDFSVNQKTA FSKLERDFEN VMIIYREDVD
FSMYDRKLSD IYHDIICEQR LRTEDKRDEY LLNLLEKELR EISKAQDSLI SMYAKKRNHA
WFDFFRNLAL LKAGEIFRCT YNTKNHGISF GEGCIYLDMD MILTGKLGTI YAPDGISMHV
DRRNDSVNIE NSAIIVNRSN HPALLEGLSF MHSKVDAHPY YDGLGKGVKK YFNFTPLHNY
NHFCDFIEFN HPNIIMNTSQ YTCSSW
