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S6 family peptidase [Shigella flexneri].


LOCUS       WP_000973741             329 aa            linear   BCT 01-MAR-2025
ACCESSION   WP_000973741
VERSION     WP_000973741.1
KEYWORDS    RefSeq.
SOURCE      Shigella flexneri
  ORGANISM  Shigella flexneri
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Shigella.
REFERENCE   1  (residues 1 to 329)
  AUTHORS   Maldonado-Contreras,A., Birtley,J.R., Boll,E., Zhao,Y., Mumy,K.L.,
            Toscano,J., Ayehunie,S., Reinecker,H.C., Stern,L.J. and
            McCormick,B.A.
  TITLE     Shigella depends on SepA to destabilize the intestinal epithelial
            integrity via cofilin activation
  JOURNAL   Gut Microbes 8 (6), 544-560 (2017)
   PUBMED   28598765
REFERENCE   2  (residues 1 to 329)
  AUTHORS   Johnson,T.A., Qiu,J., Plaut,A.G. and Holyoak,T.
  TITLE     Active-site gating regulates substrate selectivity in a
            chymotrypsin-like serine protease the structure of haemophilus
            influenzae immunoglobulin A1 protease
  JOURNAL   J Mol Biol 389 (3), 559-574 (2009)
   PUBMED   19393662
REFERENCE   3  (residues 1 to 329)
  AUTHORS   Henderson,I.R., Czeczulin,J., Eslava,C., Noriega,F. and Nataro,J.P.
  TITLE     Characterization of pic, a secreted protease of Shigella flexneri
            and enteroaggregative Escherichia coli
  JOURNAL   Infect Immun 67 (11), 5587-5596 (1999)
   PUBMED   10531204
REFERENCE   4  (residues 1 to 329)
  AUTHORS   Benjelloun-Touimi,Z., Si Tahar,M., Montecucco,C., Sansonetti,P.J.
            and Parsot,C.
  TITLE     SepA, the 110 kDa protein secreted by Shigella flexneri: two-domain
            structure and proteolytic activity
  JOURNAL   Microbiology (Reading) 144 (Pt 7), 1815-1822 (1998)
   PUBMED   9695914
REFERENCE   5  (residues 1 to 329)
  AUTHORS   Stein,M., Kenny,B., Stein,M.A. and Finlay,B.B.
  TITLE     Characterization of EspC, a 110-kilodalton protein secreted by
            enteropathogenic Escherichia coli which is homologous to members of
            the immunoglobulin A protease-like family of secreted proteins
  JOURNAL   J Bacteriol 178 (22), 6546-6554 (1996)
   PUBMED   8932311
REFERENCE   6  (residues 1 to 329)
  AUTHORS   Bachovchin,W.W., Plaut,A.G., Flentke,G.R., Lynch,M. and
            Kettner,C.A.
  TITLE     Inhibition of IgA1 proteinases from Neisseria gonorrhoeae and
            Hemophilus influenzae by peptide prolyl boronic acids
  JOURNAL   J Biol Chem 265 (7), 3738-3743 (1990)
   PUBMED   2105953
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF014452.6
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF02395.22
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..329
                     /organism="Shigella flexneri"
                     /db_xref="taxon:623"
     Protein         1..329
                     /product="S6 family peptidase"
                     /GO_function="GO:0004252 - serine-type endopeptidase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006508 - proteolysis [Evidence IEA]"
                     /calculated_mol_wt=35982
     Region          <12..>302
                     /region_name="Peptidase_S6"
                     /note="Immunoglobulin A1 protease; pfam02395"
                     /db_xref="CDD:396804"
ORIGIN      
        1 mmiykndktf rnleifgdsg sgaylydnkl ekwvlvgtth giasvngdql twitkyndkl
       61 vselkdtysh kinlngnnvt ikntditlhq nnadttgtqe kitkdkdivf tnggnvlfkd
      121 nldfgsggii fdegheynin gqrftfkgag idigkesivn wnalyssddv lhkigpgtln
      181 vqkkqganik igegnvilne egtfnniyla sgngkvilnk dnslgndqya gifftkrggt
      241 ldlnghnqtf triaatddgt titnsdtkke avlainneds yiyhgningn iklthninsq
      301 dkktnaklil dgsvntkndv evsnasltm