OSPZ_SHIBO
ID OSPZ_SHIBO Reviewed; 230 AA.
AC A0A3Z7J6R4;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Cysteine S-methyltransferase OspZ {ECO:0000305};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:A0A3T2V133};
DE AltName: Full=Effector protein OspZ {ECO:0000303|PubMed:20485572};
GN Name=ospZ {ECO:0000303|PubMed:20485572};
GN ORFNames=BL724_21090 {ECO:0000312|EMBL:EAC1015399.1};
OS Shigella boydii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=279349;
RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RC STRAIN=SBA1384;
RX PubMed=20485572; DOI=10.1371/journal.ppat.1000898;
RA Newton H.J., Pearson J.S., Badea L., Kelly M., Lucas M., Holloway G.,
RA Wagstaff K.M., Dunstone M.A., Sloan J., Whisstock J.C., Kaper J.B.,
RA Robins-Browne R.M., Jans D.A., Frankel G., Phillips A.D., Coulson B.S.,
RA Hartland E.L.;
RT "The type III effectors NleE and NleB from enteropathogenic E. coli and
RT OspZ from Shigella block nuclear translocation of NF-kappaB p65.";
RL PLoS Pathog. 6:e1000898-e1000898(2010).
CC -!- FUNCTION: Cysteine methyltransferase effector that inhibits host cell
CC NF-kappa-B activation by preventing nuclear translocation of host
CC protein RELA/p65 (PubMed:20485572). Acts by mediating cysteine
CC methylation of host proteins TAB2 and TAB3: methylation of a conserved
CC cysteine residue of the RanBP2-type zinc finger (NZF) of TAB2 and TAB3
CC disrupts zinc-binding, thereby inactivating the ubiquitin chain-binding
CC activity of TAB2 and TAB3, leading to NF-kappa-B inactivation. Also
CC mediates cysteine methylation of host protein ZRANB3, inactivating its
CC ability to bind ubiquitin chains (By similarity).
CC {ECO:0000250|UniProtKB:A0A3T2V133, ECO:0000269|PubMed:20485572}.
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:A0A3T2V133};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66545;
CC Evidence={ECO:0000250|UniProtKB:A0A3T2V133};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q7DBA6}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q2TH00}. Host
CC cytoplasm {ECO:0000250|UniProtKB:Q2TH00}. Host nucleus
CC {ECO:0000250|UniProtKB:Q2TH00}. Note=Secreted via the type III
CC secretion system (TTSS). Mainly localizes in the cytoplasm of the
CC infected cells, and occasionaly in the host nucleus.
CC {ECO:0000250|UniProtKB:Q2TH00}.
CC -!- SIMILARITY: Belongs to the NleE/OspZ family. {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; AAAGUA010000258; EAC1015399.1; -; Genomic_DNA.
DR RefSeq; WP_073832157.1; NZ_LPSW01000339.1.
DR AlphaFoldDB; A0A3Z7J6R4; -.
DR SMR; A0A3Z7J6R4; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; 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.
DR GO; GO:0085034; P:suppression by symbiont of host I-kappaB kinase/NF-kappaB cascade; IDA:UniProtKB.
PE 3: Inferred from homology;
KW Host cytoplasm; Host nucleus; Methyltransferase; S-adenosyl-L-methionine;
KW Secreted; Toxin; Transferase; Virulence.
FT CHAIN 1..230
FT /note="Cysteine S-methyltransferase OspZ"
FT /id="PRO_0000452527"
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:0000250|UniProtKB:Q7DBA6"
FT BINDING 98
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7DBA6"
FT BINDING 107
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7DBA6"
FT BINDING 111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7DBA6"
FT BINDING 204
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7DBA6"
FT BINDING 208
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q7DBA6"
SQ SEQUENCE 230 AA; 26961 MW; 8D9EC613804D315D CRC64;
MISPIKNIKN VFPINTANTE YIVRNIYPRV EHGYFNESPN IYDKKYISGI TRNMAQLKIE
EFINEKSRRL NYMKTMYSPC PEDFQPISRD EASIPEGSWL TVISGKRPMG QFSVDSLYHP
DLHALCELPE ISCKIFPKEN SDFLYIIVVF RNDSPQGELR TNRFIELYDI KREIMQVLRD
ESPELKSIKS EIIIAREMGE LFSYASEEID SYIKQMNDRF SQIKARMSVT
