ID   OSPF_SHIDS              Reviewed;         239 AA.
AC   Q327I2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Phosphothreonine lyase OspF;
DE            EC=4.2.3.-;
DE   AltName: Full=Effector protein OspF;
GN   Name=ospF; Synonyms=mkaD; OrderedLocusNames=SDY_P013;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OG   Plasmid pSD1_197.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
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 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; CP000035; ABB64526.1; -; Genomic_DNA.
DR   RefSeq; WP_001121864.1; NC_007607.1.
DR   RefSeq; YP_406014.1; NC_007607.1.
DR   AlphaFoldDB; Q327I2; -.
DR   SMR; Q327I2; -.
DR   EnsemblBacteria; ABB64526; ABB64526; SDY_P013.
DR   KEGG; sdy:SDY_P013; -.
DR   HOGENOM; CLU_100525_0_0_6; -.
DR   OMA; RVDQQSR; -.
DR   Proteomes; UP000002716; Plasmid pSD1_197.
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; Reference proteome; Secreted; Virulence.
FT   CHAIN           1..239
FT                   /note="Phosphothreonine lyase OspF"
FT                   /id="PRO_0000299352"
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;  27900 MW;  95A9F09DD94D1A3B CRC64;
     MPIKKPCLKL NLDSLNVVRS EIPQMLSANE RLKNNFNILY NQIRQYPAYY FKVASNVPNY
     SDICQFFSVM YQGFQIVNHS GDVFIHACRE NPQSKGDFVG DKFHISIARE QVPLAFQILS
     GLLFSEDSPI DKWKITDMNR VSQQSRVGIG AQFTLYVKSD QECSQYSALL LHKIRQFIMC
     LESNLLRSKI APGEYPASDV RPEDWKYVSY RNELRSDRNG SERQEQMLRE EPFYRLMIE