ID   OSPF_SHIBS              Reviewed;         239 AA.
AC   Q31SR9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Phosphothreonine lyase OspF;
DE            EC=4.2.3.-;
DE   AltName: Full=Effector protein OspF;
GN   Name=ospF; Synonyms=mkaD; OrderedLocusNames=SBO_P017;
OS   Shigella boydii serotype 4 (strain Sb227).
OG   Plasmid pSB4_227.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300268;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sb227;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: Catalyzes the removal of the phosphate group from the
CC       phosphothreonine in the mitogen-activated protein kinases p38,
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}.
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; CP000037; ABB68889.1; -; Genomic_DNA.
DR   RefSeq; WP_001121865.1; NC_007608.1.
DR   AlphaFoldDB; Q31SR9; -.
DR   SMR; Q31SR9; -.
DR   EnsemblBacteria; ABB68889; ABB68889; SBO_P017.
DR   GeneID; 58463867; -.
DR   KEGG; sbo:SBO_P017; -.
DR   HOGENOM; CLU_100525_0_0_6; -.
DR   OMA; RVDQQSR; -.
DR   Proteomes; UP000007067; Plasmid pSB4_227.
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..239
FT                   /note="Phosphothreonine lyase OspF"
FT                   /id="PRO_0000299351"
FT   ACT_SITE        104
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        134
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   239 AA;  27888 MW;  7A53F087DFF6AA8B CRC64;
     MPIKKPCLKL NLDSLNVVRS EIPQMLSANE RLKNNFNILY NQIRQYPAYY FKVASNVPTY
     SDICQFFSVM YQGFQIVNHS GDVFIHACRE NPQSKGDFVG DKFHISIARE QVPLAFQILS
     GLLFSEDSPI DKWKITDMNR VSQQSRVGIG AQFTLYVKSD QECSQYSALL LHKIRQFIMC
     LESNLLRSKI APGEYPASDV RPEDWKYVSY RNELRSDRDG SERQEQMLRE EPFYRLMIE