OSPF_SHIDY
ID OSPF_SHIDY Reviewed; 170 AA.
AC Q2ET08;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Phosphothreonine lyase OspF;
DE EC=4.2.3.-;
DE AltName: Full=Effector protein OspF;
DE Flags: Fragment;
GN Name=ospF;
OS Shigella dysenteriae.
OG Plasmid pSd9_G1274, Plasmid pSd11_G1246, Plasmid pSd12_G1263,
OG Plasmid pSd13_G1271, Plasmid pSd2_G1252, Plasmid pSd3_G1281,
OG Plasmid pSd4_G1190, Plasmid pSd5_G1213, Plasmid pSd6_G1192, and
OG Plasmid pSd7_G1222.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=622;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=G1190 / Serotype 4, G1192 / Serotype 6, G1213 / Serotype 5,
RC G1222 / Serotype 7, G1246 / Serotype 11, G1252 / Serotype 2,
RC G1263 / Serotype 12, G1271 / Serotype 13, G1274 / Serotype 9, and
RC G1281 / Serotype 3;
RC PLASMID=pSd11_G1246, pSd12_G1263, pSd13_G1271, pSd2_G1252, pSd3_G1281,
RC pSd4_G1190, pSd5_G1213, pSd6_G1192, pSd7_G1222, and pSd9_G1274;
RX PubMed=17160643; DOI=10.1007/s00239-006-0052-8;
RA Yang J., Nie H., Chen L., Zhang X., Yang F., Xu X., Zhu Y., Yu J., Jin Q.;
RT "Revisiting the molecular evolutionary history of Shigella spp.";
RL J. Mol. Evol. 64:71-79(2007).
CC -!- FUNCTION: Catalyzes the removal of the phosphate group from the
CC phosphothreonine in the mitogen-activated protein kinases such as
CC MAPK2/ERK2, MAPK3/ERK1, MAPK8 and MAPK14 in an irreversible reaction,
CC thus preventing the downstream phosphorylation of histone H3. This
CC epigenetic modification results in inhibition of the transcription of a
CC specific subset of pro-inflammatory genes, and ultimately to a reduced
CC immune response against the invading pathogen. The diminished immune
CC response enhances the bacterium's ability to disseminate and multiply
CC within the host (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted via the type III
CC secretion system (TTSS). Localizes in the nucleus of the infected cell
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphothreonine lyase family.
CC {ECO:0000305}.
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DR EMBL; DQ362871; ABD37278.1; -; Genomic_DNA.
DR EMBL; DQ362872; ABD37279.1; -; Genomic_DNA.
DR EMBL; DQ362873; ABD37280.1; -; Genomic_DNA.
DR EMBL; DQ362874; ABD37281.1; -; Genomic_DNA.
DR EMBL; DQ362875; ABD37282.1; -; Genomic_DNA.
DR EMBL; DQ362876; ABD37283.1; -; Genomic_DNA.
DR EMBL; DQ362877; ABD37284.1; -; Genomic_DNA.
DR EMBL; DQ362878; ABD37285.1; -; Genomic_DNA.
DR EMBL; DQ362879; ABD37286.1; -; Genomic_DNA.
DR EMBL; DQ362880; ABD37287.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2ET08; -.
DR SMR; Q2ET08; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.2430.10; -; 1.
DR InterPro; IPR003519; OspF/SpvC.
DR InterPro; IPR038498; OspF/SpvC_sf.
DR Pfam; PF03536; VRP3; 1.
DR PRINTS; PR01342; SALVRPPROT.
PE 3: Inferred from homology;
KW Lyase; Plasmid; Secreted; Virulence.
FT CHAIN <1..>170
FT /note="Phosphothreonine lyase OspF"
FT /id="PRO_0000299353"
FT ACT_SITE 82
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 112
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 170
SQ SEQUENCE 170 AA; 19585 MW; B2D0850BF4172738 CRC64;
PQMLSANERL KNNFNILYNQ IRQYPAYYFK VASNVPTYSD ICQFFSVMYQ GFQIVNHSGD
VFIHACRENP QSKGDFVGDK FHISIAREQV PLAFQILSGL LFSEDSPIDK WKITDMNRVS
QQSRVGIGAQ FTLYVKSDQE CSQYSALLLH KIRQFIMCLE SNLLRSKIAP
