NLEB2_ECO27
ID NLEB2_ECO27 Reviewed; 326 AA.
AC B7UNX3;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Protein-arginine N-acetylglucosaminyltransferase NleB2 {ECO:0000305};
DE Short=Arginine GlcNAcyltransferase NleB2 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000269|PubMed:23955153};
DE AltName: Full=Non-LEE-encoded type III effector B2 {ECO:0000303|PubMed:23955153};
GN Name=nleB2 {ECO:0000303|PubMed:23955153};
GN OrderedLocusNames=E2348C_1041 {ECO:0000312|EMBL:CAS08589.1};
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, AND CATALYTIC ACTIVITY.
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 [3]
RP FUNCTION.
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 [4]
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).
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 (PubMed:23955153).
CC In contrast to NleB1, not able to disrupt TNF signaling in infected
CC cells (PubMed:23955153, PubMed:24025841, PubMed:28522607). Shows a
CC lower enzymatic activity than NleB1 (PubMed:23955153).
CC {ECO:0000269|PubMed:23955153, ECO:0000269|PubMed:24025841,
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:0000269|PubMed:23955153};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66633;
CC Evidence={ECO:0000269|PubMed:23955153};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FM180568; CAS08589.1; -; Genomic_DNA.
DR RefSeq; WP_000950813.1; NC_011601.1.
DR AlphaFoldDB; B7UNX3; -.
DR SMR; B7UNX3; -.
DR DIP; DIP-60596N; -.
DR IntAct; B7UNX3; 1.
DR EnsemblBacteria; CAS08589; CAS08589; E2348C_1041.
DR KEGG; ecg:E2348C_1041; -.
DR HOGENOM; CLU_081850_0_0_6; -.
DR Proteomes; UP000008205; 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 1: Evidence at protein level;
KW Glycosyltransferase; Manganese; Metal-binding; Secreted; Toxin;
KW Transferase; Virulence.
FT CHAIN 1..326
FT /note="Protein-arginine N-acetylglucosaminyltransferase
FT NleB2"
FT /id="PRO_0000452593"
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
