ICSP_SHIFL
ID ICSP_SHIFL Reviewed; 315 AA.
AC O33641; P95750; Q6XW13; Q7BEI2;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Outer membrane protease IcsP;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN Name=icsP; Synonyms=sopA; OrderedLocusNames=CP0271;
OS Shigella flexneri.
OG Plasmid pWR100, Plasmid pCP301, and Plasmid pINV_F6_M1382.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=9076742; DOI=10.1046/j.1365-2958.1997.2871652.x;
RA Egile C., d'Hauteville H., Parsot C., Sansonetti P.J.;
RT "SopA, the outer membrane protease responsible for polar localization of
RT IcsA in Shigella flexneri.";
RL Mol. Microbiol. 23:1063-1073(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; PLASMID=pWR100;
RX PubMed=9302008; DOI=10.1046/j.1365-2958.1997.4681827.x;
RA Shere K.D., Sallustio S., Manessis A., D'Aversa T.G., Goldberg M.B.;
RT "Disruption of IcsP, the major Shigella protease that cleaves IcsA,
RT accelerates actin-based motility.";
RL Mol. Microbiol. 25:451-462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M1382 / Serotype 6; PLASMID=pINV_F6_M1382;
RX PubMed=14573649; DOI=10.1128/iai.71.11.6298-6306.2003;
RA Lan R., Stevenson G., Reeves P.R.;
RT "Comparison of two major forms of the Shigella virulence plasmid pINV:
RT positive selection is a major force driving the divergence.";
RL Infect. Immun. 71:6298-6306(2003).
RN [6]
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 [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a, and M90T / Serotype 5a;
RC PLASMID=pWR100;
RX PubMed=10231492; DOI=10.1046/j.1365-2958.1999.01356.x;
RA Steinhauer J., Agha R., Pham T., Varga A.W., Goldberg M.B.;
RT "The unipolar Shigella surface protein IcsA is targeted directly to the
RT bacterial old pole: IcsP cleavage of IcsA occurs over the entire bacterial
RT surface.";
RL Mol. Microbiol. 32:367-377(1999).
RN [8]
RP REGULATION BY VIRB.
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a; PLASMID=pWR100;
RX PubMed=14729695; DOI=10.1128/jb.186.3.699-705.2004;
RA Wing H.J., Yan A.W., Goldman S.R., Goldberg M.B.;
RT "Regulation of IcsP, the outer membrane protease of the Shigella actin tail
RT assembly protein IcsA, by virulence plasmid regulators VirF and VirB.";
RL J. Bacteriol. 186:699-705(2004).
CC -!- FUNCTION: Protease responsible for the cleavage of IcsA between 'Arg-
CC 758' and 'Arg-759', removing the entire alpha domain from IscA
CC localized on the bacterial surface. This proteolytic activity
CC contributes to the maintenance of a tight polar cap of IcsA, which is
CC important to Shigella actin-based motility.
CC {ECO:0000269|PubMed:10231492, ECO:0000269|PubMed:9076742,
CC ECO:0000269|PubMed:9302008}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000269|PubMed:10231492}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10231492}.
CC -!- INDUCTION: Transcriptionally regulated by VirB (InvE).
CC -!- SIMILARITY: Belongs to the peptidase A26 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB61737.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAK18603.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U73461; AAC45084.1; -; Genomic_DNA.
DR EMBL; AF001633; AAB61737.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL391753; CAC05769.2; -; Genomic_DNA.
DR EMBL; AF348706; AAK18603.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY206427; AAP78966.1; -; Genomic_DNA.
DR EMBL; AF386526; AAL72459.2; -; Genomic_DNA.
DR RefSeq; NP_858404.2; NC_004851.1.
DR RefSeq; WP_005061047.1; NZ_WPGT01000123.1.
DR RefSeq; YP_009062451.1; NC_024996.1.
DR AlphaFoldDB; O33641; -.
DR SMR; O33641; -.
DR STRING; 198214.CP0271; -.
DR MEROPS; A26.005; -.
DR EnsemblBacteria; AAL72459; AAL72459; SF_p0271.
DR GeneID; 1238162; -.
DR KEGG; sfl:CP0271; -.
DR PATRIC; fig|198214.7.peg.5532; -.
DR HOGENOM; CLU_063041_1_0_6; -.
DR OMA; HENFEFG; -.
DR PHI-base; PHI:6577; -.
DR Proteomes; UP000001006; Plasmid pCP301.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR020080; OM_adhesin/peptidase_omptin.
DR InterPro; IPR020079; Peptidase_A26_CS.
DR InterPro; IPR000036; Peptidase_A26_omptin.
DR Pfam; PF01278; Omptin; 1.
DR PIRSF; PIRSF001522; Peptidase_A26; 1.
DR PRINTS; PR00482; OMPTIN.
DR SUPFAM; SSF69917; SSF69917; 1.
DR PROSITE; PS00834; OMPTIN_1; 1.
DR PROSITE; PS00835; OMPTIN_2; 1.
PE 2: Evidence at transcript level;
KW Aspartyl protease; Cell outer membrane; Hydrolase; Membrane; Plasmid;
KW Protease; Reference proteome; Signal; Transmembrane;
KW Transmembrane beta strand; Virulence.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..315
FT /note="Outer membrane protease IcsP"
FT /id="PRO_0000025820"
FT ACT_SITE 103
FT /evidence="ECO:0000250"
FT ACT_SITE 105
FT /evidence="ECO:0000250"
FT ACT_SITE 230
FT /evidence="ECO:0000250"
FT ACT_SITE 232
FT /evidence="ECO:0000250"
FT VARIANT 6
FT /note="F -> L (in plasmid pINV_F6_M1382)"
FT VARIANT 176
FT /note="S -> N (in plasmid pINV_F6_M1382)"
FT VARIANT 182
FT /note="A -> T (in plasmid pINV_F6_M1382)"
FT VARIANT 225
FT /note="L -> R (in plasmid pINV_F6_M1382)"
SQ SEQUENCE 315 AA; 35597 MW; 26E4C4B091A644E8 CRC64;
MKLKFFVLAL CVPAIFTTHA TTNYPLFIPD NISTDISLGS LSGKTKERVY HPKEGGRKIS
QLDWKYSNAT IVRGGIDWKL IPKVSFGVSG WTTLGNQKAS MVDKDWNNSN TPQVWTDQSW
HPNTHLRDAN EFELNLKGWL LNNLDYRLGL IAGYQESRYS FNAMGGSYIY SENGGSRNKK
GAHPSGERTI GYKQLFKIPY IGLTANYRHE NFEFGAELKY SGWVLSSDTD KHYQTETIFK
DEIKNQNYCS VAANIGYYVT PSAKFYIEGS RNYISNKKGD TSLYEQSTNI SGTIKNSASI
EYIGFLTSAG IKYIF
