ID   VIRA_SHISS              Reviewed;         400 AA.
AC   Q3YTK0;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Cysteine protease-like VirA;
DE            EC=3.4.22.-;
DE   AltName: Full=Effector protein VirA;
GN   Name=virA; OrderedLocusNames=SSON_P142;
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: Alpha-tubulin-specific protease that is required for entry
CC       into epithelial cells and for subsequent intra- and intercellular
CC       spreading. Contributes to bacterial entry into epithelial cells by
CC       inducing microtubule (MT) destabilization and the formation of membrane
CC       ruffles. The membrane ruffling evoked by VirA results from the
CC       activation of host rac1, which is associated with the destruction of MT
CC       networks. Creates a tunnel inside the host cell cytoplasm by breaking
CC       down the microtubule infrastructure. This facilitates the bacterium's
CC       movement through the cytoplasm and also helps other bacteria move
CC       faster during the invasion of the eukaryotic cell. Is absolutely
CC       required for virulence (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. Interacts specifically with alpha tubulin, a major
CC       component of microtubule (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Translocated into the host cell
CC       via the type III secretion system (TTSS). Localizes in the cytoplasm of
CC       the infected cell (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protease EspG/VirA family. {ECO:0000305}.
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DR   EMBL; CP000039; AAZ91162.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3YTK0; -.
DR   SMR; Q3YTK0; -.
DR   EnsemblBacteria; AAZ91162; AAZ91162; SSON_P142.
DR   KEGG; ssn:SSON_P142; -.
DR   HOGENOM; CLU_688663_0_0_6; -.
DR   OMA; KCEIDEM; -.
DR   Proteomes; UP000002529; Plasmid pSS_046.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.450.460; -; 1.
DR   InterPro; IPR009669; Cys_protease_VirA/EspG.
DR   InterPro; IPR043098; Cys_protease_VirA/EspG_N.
DR   Pfam; PF06872; EspG; 1.
DR   PIRSF; PIRSF011515; EspG; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Plasmid; Protease; Secreted; Thiol protease; Virulence.
FT   CHAIN           1..400
FT                   /note="Cysteine protease-like VirA"
FT                   /id="PRO_0000297844"
FT   REGION          224..315
FT                   /note="Tubulin-binding domain"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        34
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   400 AA;  44706 MW;  9F392334FB30C32E CRC64;
     MQTSNITNHE RNDSSWMSTV KSTTEVSWNK LSFCDVLLKI ITFGIYSPHE TLAEKYSEKK
     LMDSFSPSLS QDKMDGEFAH ANIDGISIRL CLNKGICSVF YLDGDKIQST QLSSKEYNNL
     LSSLPPKQFN LGKVHTITAP VSGNFKTHKP APEVIETAIN CCTSIIPNDD YFPVKDTDFN
     SVWHDIYRDI RASNSNSTKI YFNNIEIPLK LIADLINELG INEFIDSKKE LQMLSYNQVN
     KIINSNFPQQ DLCFQTEKLL FTSLFQDPAF ISALTSAFWQ SLHITSSSVE HIYAQIMSEN
     IENRLNFMPE QRVINNCGHI IKINAVVPKN DTAISASGGR AYEVSSSILP SHITCNGVGI
     NKIETSYLVH AGTLPSSEGL RNAIPPESRQ VSFAIISPDV