ID   VIRA_SHIDS              Reviewed;         400 AA.
AC   Q326N4;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Cysteine protease-like VirA;
DE            EC=3.4.22.-;
DE   AltName: Full=Effector protein VirA;
GN   Name=virA; OrderedLocusNames=SDY_P211;
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: 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; CP000035; ABB64724.1; -; Genomic_DNA.
DR   RefSeq; WP_001195011.1; NC_007607.1.
DR   RefSeq; YP_406212.1; NC_007607.1.
DR   AlphaFoldDB; Q326N4; -.
DR   SMR; Q326N4; -.
DR   EnsemblBacteria; ABB64724; ABB64724; SDY_P211.
DR   KEGG; sdy:SDY_P211; -.
DR   PATRIC; fig|300267.13.peg.5765; -.
DR   HOGENOM; CLU_688663_0_0_6; -.
DR   OMA; KCEIDEM; -.
DR   Proteomes; UP000002716; Plasmid pSD1_197.
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; Reference proteome; Secreted; Thiol protease;
KW   Virulence.
FT   CHAIN           1..400
FT                   /note="Cysteine protease-like VirA"
FT                   /id="PRO_0000297843"
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;  44723 MW;  B02250769B731B39 CRC64;
     MQTSNITNYE RNDSSWMSTV KSTTEVSWNK LSFCDVLLKI ITFGIYSPHE TLAEKYSEKK
     LMDSFSPSLS QDKMDGEFAH ANIDGISIRL CLNKGICSVF YLDGDKIQST QLSSKEYNNL
     LSSLPPKQFN LGKVHTITAP VSGNFKTHKP APEVIETAIN CCTSIIPNDD YFSVKDTDFN
     SVWHDIYRDI RASDSNSTKI YFNNIEIPLK LIADLINELG INEFIDSKKE LQMLSYNQVN
     KIINSNFPQQ DLCFQTEKLL FTSLFQDPAF ISALTSAFWQ SLHITSSSVE HIYAQIMSEN
     IENRLNFMPE QRVINNCGHI IKINAVVPKN DTAISASGGR AYEVSSSILP SHITCNGVGI
     NKIETSYLVH AGTLPSSEGL RNAIPPESRQ VSFAIISPDV