NLEE_ECO57
ID NLEE_ECO57 Reviewed; 224 AA.
AC Q7DBA6; A0A0H3JGS9; A0A6M0JHE4; Q7AAU9;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Cysteine S-methyltransferase NleE {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:B7UI22};
DE AltName: Full=Effector protein NleE {ECO:0000250|UniProtKB:B7UI22};
DE AltName: Full=Non-LEE-encoded type III effector E {ECO:0000250|UniProtKB:B7UI22};
GN Name=nleE {ECO:0000303|PubMed:25412445};
GN ORFNames=ECs_3858 {ECO:0000312|EMBL:BAB37281.1};
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
RC {ECO:0000312|Proteomes:UP000000558};
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] {ECO:0007744|PDB:4R29}
RP X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE, AND SUBUNIT.
RX PubMed=25412445; DOI=10.1371/journal.ppat.1004522;
RA Yao Q., Zhang L., Wan X., Chen J., Hu L., Ding X., Li L., Karar J.,
RA Peng H., Chen S., Huang N., Rauscher F.J. III, Shao F.;
RT "Structure and specificity of the bacterial cysteine methyltransferase
RT effector NleE suggests a novel substrate in human DNA repair pathway.";
RL PLoS Pathog. 10:e1004522-e1004522(2014).
CC -!- FUNCTION: Cysteine methyltransferase effector that inhibits host cell
CC NF-kappa-B activation by preventing nuclear translocation of host
CC protein RELA/p65. Acts by mediating cysteine methylation of host
CC proteins TAB2 and TAB3: methylation of a conserved cysteine residue of
CC the RanBP2-type zinc finger (NZF) of TAB2 and TAB3 disrupts zinc-
CC binding, thereby inactivating the ubiquitin chain-binding activity of
CC TAB2 and TAB3, leading to NF-kappa-B inactivation. Also mediates
CC cysteine methylation of host protein ZRANB3, inactivating its ability
CC to bind ubiquitin chains. {ECO:0000250|UniProtKB:B7UI22}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + S-adenosyl-L-methionine = H(+) + S-
CC adenosyl-L-homocysteine + S-methyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:66544, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:82612;
CC Evidence={ECO:0000250|UniProtKB:B7UI22};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66545;
CC Evidence={ECO:0000250|UniProtKB:B7UI22};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:25412445}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:B7UI22}. Host
CC nucleus {ECO:0000250|UniProtKB:B7UI22}. Note=Secreted via the type III
CC secretion system (TTSS). Localizes in the nucleus of the infected
CC cells. {ECO:0000250|UniProtKB:B7UI22}.
CC -!- SIMILARITY: Belongs to the NleE/OspZ family. {ECO:0000305}.
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DR EMBL; BA000007; BAB37281.1; -; Genomic_DNA.
DR RefSeq; NP_311885.1; NC_002695.1.
DR RefSeq; WP_000609742.1; NZ_SWKA01000005.1.
DR PDB; 4R29; X-ray; 2.31 A; A/B/C/D=1-224.
DR PDBsum; 4R29; -.
DR AlphaFoldDB; Q7DBA6; -.
DR SMR; Q7DBA6; -.
DR EnsemblBacteria; BAB37281; BAB37281; ECs_3858.
DR EnsemblBacteria; QCH81150; QCH81150; CAM50_0004300.
DR GeneID; 916318; -.
DR KEGG; ecs:ECs_3858; -.
DR PATRIC; fig|386585.9.peg.4026; -.
DR eggNOG; ENOG5033TQ0; Bacteria.
DR HOGENOM; CLU_1347196_0_0_6; -.
DR OMA; TANTEYI; -.
DR Proteomes; UP000000558; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Host nucleus; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Secreted; Toxin; Transferase; Virulence.
FT CHAIN 1..224
FT /note="Cysteine S-methyltransferase NleE"
FT /id="PRO_0000452525"
FT REGION 49..52
FT /note="Interaction with host proteins TAB2, TAB3 and
FT ZRANB3"
FT /evidence="ECO:0000250|UniProtKB:B7UI22"
FT BINDING 92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:25412445,
FT ECO:0007744|PDB:4R29"
FT BINDING 98
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:25412445,
FT ECO:0007744|PDB:4R29"
FT BINDING 107
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:25412445,
FT ECO:0007744|PDB:4R29"
FT BINDING 111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:25412445,
FT ECO:0007744|PDB:4R29"
FT BINDING 204
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:25412445,
FT ECO:0007744|PDB:4R29"
FT BINDING 208
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:25412445,
FT ECO:0007744|PDB:4R29"
FT HELIX 22..26
FT /evidence="ECO:0007829|PDB:4R29"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:4R29"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:4R29"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:4R29"
FT HELIX 63..76
FT /evidence="ECO:0007829|PDB:4R29"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:4R29"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:4R29"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:4R29"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:4R29"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:4R29"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:4R29"
FT HELIX 156..181
FT /evidence="ECO:0007829|PDB:4R29"
FT HELIX 186..201
FT /evidence="ECO:0007829|PDB:4R29"
FT HELIX 206..219
FT /evidence="ECO:0007829|PDB:4R29"
SQ SEQUENCE 224 AA; 26058 MW; 0105F0BE325AF5C8 CRC64;
MINPVTNTQG VSPINTKYAE HVVKNIYPEI KHDYFNESPN IYDKKYISGI TRGVAELKQE
EFVNEKARRF SYMKTMYSVC PEAFEPISRN EASTPEGSWL TVISGKRPMG QFSVDSLYNP
DLHALCELPD ICCKIFPKEN NDFLYIVVVY RNDSPLGEQR ANRFIELYNI KRDIMQELNY
ELPELKAVKS EMIIAREMGE IFSYMPGEID SYMKYINNKL SKIE
