OSPG_SHISS
ID OSPG_SHISS Reviewed; 196 AA.
AC Q3YTH2;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Protein kinase OspG;
DE EC=2.7.-.-;
DE AltName: Full=Effector protein OspG;
GN Name=ospG; OrderedLocusNames=SSON_P170;
OS Shigella sonnei (strain Ss046).
OG Plasmid pSS_046.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16122562; DOI=10.1016/j.plasmid.2005.03.002;
RA Jiang Y., Yang F., Zhang X., Yang J., Chen L., Yan Y., Nie H., Xiong Z.,
RA Wang J., Dong J., Xue Y., Xu X., Zhu Y., Chen S., Jin Q.;
RT "The complete sequence and analysis of the large virulence plasmid pSS of
RT Shigella sonnei.";
RL Plasmid 54:149-159(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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Host cell {ECO:0000250}.
CC Note=Secreted via Mxi-Spa type III secretion system (TTSS), and
CC delivered into the host cell. {ECO:0000250}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
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DR EMBL; CP000039; AAZ91190.1; -; Genomic_DNA.
DR PDB; 4Q5E; X-ray; 1.87 A; A=26-196.
DR PDB; 4Q5H; X-ray; 2.00 A; A=26-196.
DR PDBsum; 4Q5E; -.
DR PDBsum; 4Q5H; -.
DR AlphaFoldDB; Q3YTH2; -.
DR SMR; Q3YTH2; -.
DR EnsemblBacteria; AAZ91190; AAZ91190; SSON_P170.
DR KEGG; ssn:SSON_P170; -.
DR HOGENOM; CLU_120872_0_0_6; -.
DR OMA; YTEYYSA; -.
DR Proteomes; UP000002529; Plasmid pSS_046.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0043657; C:host cell; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Kinase; Phosphoprotein; Plasmid; Secreted; Transferase;
KW Virulence.
FT CHAIN 1..196
FT /note="Protein kinase OspG"
FT /id="PRO_0000395880"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:4Q5E"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:4Q5E"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:4Q5E"
FT HELIX 62..80
FT /evidence="ECO:0007829|PDB:4Q5E"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:4Q5E"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:4Q5E"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:4Q5E"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:4Q5E"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:4Q5E"
FT HELIX 118..131
FT /evidence="ECO:0007829|PDB:4Q5E"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:4Q5E"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:4Q5E"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:4Q5E"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:4Q5E"
FT HELIX 162..167
FT /evidence="ECO:0007829|PDB:4Q5E"
FT HELIX 170..191
FT /evidence="ECO:0007829|PDB:4Q5E"
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
