OSPG_SHIFL
ID OSPG_SHIFL Reviewed; 196 AA.
AC Q99PZ6; Q7BCI9; Q7BEJ9;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Protein kinase OspG;
DE EC=2.7.-.-;
DE AltName: Full=Effector protein OspG;
GN Name=ospG; OrderedLocusNames=CP0227; ORFNames=pWR501_0237, SFLP087;
OS Shigella flexneri.
OG Plasmid pCP301, Plasmid pWR100, and Plasmid pSF5.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-9, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=11115111; DOI=10.1046/j.1365-2958.2000.02179.x;
RA Buchrieser C., Glaser P., Rusniok C., Nedjari H., d'Hauteville H.,
RA Kunst F., Sansonetti P.J., Parsot C.;
RT "The virulence plasmid pWR100 and the repertoire of proteins secreted by
RT the type III secretion apparatus of Shigella flexneri.";
RL Mol. Microbiol. 38:760-771(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=11292750; DOI=10.1128/iai.69.5.3271-3285.2001;
RA Venkatesan M.M., Goldberg M.B., Rose D.J., Grotbeck E.J., Burland V.,
RA Blattner F.R.;
RT "Complete DNA sequence and analysis of the large virulence plasmid of
RT Shigella flexneri.";
RL Infect. Immun. 69:3271-3285(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serotype 5; PLASMID=pSF5;
RX PubMed=16704117; DOI=10.1007/s11427-006-0141-3;
RA Xiong Z., Tang X., Yang F., Zhang X., Yang J., Chen L., Nie H., Yan Y.,
RA Jiang Y., Wang J., Xue Y., Xu X., Zhu Y., Dong J., An L., Wang X., Jin Q.;
RT "Comparison of the virulence plasmid genomes of two strains of Shigella
RT which lost the ability to bind Congo red.";
RL Sci. China, Ser. C, Life Sci. 49:141-148(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a; PLASMID=pCP301;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [5]
RP FUNCTION, SUBUNIT, PTM, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-53.
RC STRAIN=M90T / Serotype 5a;
RX PubMed=16162672; DOI=10.1073/pnas.0504466102;
RA Kim D.W., Lenzen G., Page A.L., Legrain P., Sansonetti P.J., Parsot C.;
RT "The Shigella flexneri effector OspG interferes with innate immune
RT responses by targeting ubiquitin-conjugating enzymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:14046-14051(2005).
CC -!- FUNCTION: Effector proteins function to alter host cell physiology and
CC promote bacterial survival in host tissues. This protein is a kinase
CC that is involved in down-regulation of the host innate response induced
CC by invasive bacteria. Prevents or at least delays host phospho-NF-
CC kappa-B inhibitor alpha (NFKBIA) degradation. Does not phosphorylate E2
CC enzymes. {ECO:0000269|PubMed:16162672}.
CC -!- SUBUNIT: Binds various host ubiquitinated E2 ubiquitin-conjugating
CC enzymes, including UBE2D2 (UBCH5B). {ECO:0000269|PubMed:16162672}.
CC -!- INTERACTION:
CC Q99PZ6; P62837: UBE2D2; Xeno; NbExp=3; IntAct=EBI-9316527, EBI-347677;
CC Q99PZ6; P61077: UBE2D3; Xeno; NbExp=6; IntAct=EBI-9316527, EBI-348268;
CC Q99PZ6; P51965: UBE2E1; Xeno; NbExp=3; IntAct=EBI-9316527, EBI-348546;
CC Q99PZ6; Q96LR5: UBE2E2; Xeno; NbExp=2; IntAct=EBI-9316527, EBI-2129763;
CC Q99PZ6; P61086: UBE2K; Xeno; NbExp=2; IntAct=EBI-9316527, EBI-473850;
CC Q99PZ6; P68036: UBE2L3; Xeno; NbExp=3; IntAct=EBI-9316527, EBI-711173;
CC Q99PZ6; P68036-1: UBE2L3; Xeno; NbExp=4; IntAct=EBI-9316527, EBI-15556257;
CC Q99PZ6; O14933: UBE2L6; Xeno; NbExp=2; IntAct=EBI-9316527, EBI-2129974;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11115111}. Host cell
CC {ECO:0000305|PubMed:11115111}. Note=Secreted via Mxi-Spa type III
CC secretion system (TTSS), and delivered into the host cell.
CC {ECO:0000305}.
CC -!- PTM: Autophosphorylated.
CC -!- DISRUPTION PHENOTYPE: Mutant induces a stronger inflammatory reaction
CC upon infection. {ECO:0000269|PubMed:16162672}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
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DR EMBL; AF386526; AAL72314.1; -; Genomic_DNA.
DR EMBL; AF348706; AAK18547.1; -; Genomic_DNA.
DR EMBL; AY879342; AAW64846.1; -; Genomic_DNA.
DR EMBL; AL391753; CAC05855.1; -; Genomic_DNA.
DR RefSeq; NP_085391.1; NC_002698.1.
DR RefSeq; NP_858360.1; NC_004851.1.
DR RefSeq; WP_000705601.1; NZ_WPGW01000288.1.
DR RefSeq; YP_006960315.1; NC_019197.1.
DR RefSeq; YP_009062537.1; NC_024996.1.
DR PDB; 4BVU; X-ray; 2.70 A; A=1-196.
DR PDBsum; 4BVU; -.
DR AlphaFoldDB; Q99PZ6; -.
DR SMR; Q99PZ6; -.
DR DIP; DIP-60998N; -.
DR IntAct; Q99PZ6; 11.
DR MINT; Q99PZ6; -.
DR STRING; 198214.CP0227; -.
DR EnsemblBacteria; AAL72314; AAL72314; SF_p0227.
DR GeneID; 1238010; -.
DR KEGG; sfl:CP0227; -.
DR PATRIC; fig|198214.7.peg.5485; -.
DR HOGENOM; CLU_120872_0_0_6; -.
DR OMA; YTEYYSA; -.
DR PRO; PR:Q99PZ6; -.
DR Proteomes; UP000001006; Plasmid pCP301.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0043657; C:host cell; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Kinase; Phosphoprotein; Plasmid;
KW Reference proteome; Secreted; Transferase; Virulence.
FT CHAIN 1..196
FT /note="Protein kinase OspG"
FT /id="PRO_0000395877"
FT MUTAGEN 53
FT /note="K->A: Lack of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:16162672"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:4BVU"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:4BVU"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:4BVU"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:4BVU"
FT HELIX 62..80
FT /evidence="ECO:0007829|PDB:4BVU"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:4BVU"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:4BVU"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:4BVU"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:4BVU"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:4BVU"
FT HELIX 118..131
FT /evidence="ECO:0007829|PDB:4BVU"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:4BVU"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:4BVU"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:4BVU"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:4BVU"
FT HELIX 162..167
FT /evidence="ECO:0007829|PDB:4BVU"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:4BVU"
FT HELIX 173..193
FT /evidence="ECO:0007829|PDB:4BVU"
SQ SEQUENCE 196 AA; 22570 MW; E90908CB43BCB28A CRC64;
MKITSTIIQT PFPFENNNSH AGIVTEPILG KLIGQGSTAE IFEDVNDSSA LYKKYDLIGN
QYNEILEMAW QESELFNAFY GDEASVVIQY GGDVYLRMLR VPGTPLSDID TADIPDNIES
LYLQLICKLN ELSIIHYDLN TGNMLYDKES ESLFPIDFRN IYAEYYAATK KDKEIIDRRL
QMRTNDFYSL LNRKYL
