IPAJ_SHIFL
ID IPAJ_SHIFL Reviewed; 259 AA.
AC Q54150; Q7BEM0; Q8VSI0;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Cysteine protease IpaJ;
DE EC=3.4.22.-;
DE AltName: Full=Effector protein IpaJ;
DE AltName: Full=Invasion plasmid antigen J;
GN Name=ipaJ; OrderedLocusNames=CP0122; ORFNames=pWR501_0130;
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], INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=9441862; DOI=10.1006/mpat.1997.0164;
RA Buysse J.M., Dunyak D.S., Hartman A.B., Venkatesan M.M.;
RT "Identification and molecular characterization of a 27 kDa Shigella
RT flexneri invasion plasmid antigen, IpaJ.";
RL Microb. Pathog. 23:357-369(1997).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP SUBCELLULAR LOCATION, AND SECRETION VIA TYPE III SECRETION SYSTEM.
RX PubMed=18208325; DOI=10.1371/journal.ppat.0040009;
RA Slagowski N.L., Kramer R.W., Morrison M.F., LaBaer J., Lesser C.F.;
RT "A functional genomic yeast screen to identify pathogenic bacterial
RT proteins.";
RL PLoS Pathog. 4:E9-E9(2008).
RN [7]
RP FUNCTION, MUTAGENESIS OF CYS-64; HIS-206 AND ASP-218, AND ACTIVE SITE.
RX PubMed=23535599; DOI=10.1038/nature12004;
RA Burnaevskiy N., Fox T.G., Plymire D.A., Ertelt J.M., Weigele B.A.,
RA Selyunin A.S., Way S.S., Patrie S.M., Alto N.M.;
RT "Proteolytic elimination of N-myristoyl modifications by the Shigella
RT virulence factor IpaJ.";
RL Nature 496:106-109(2013).
CC -!- FUNCTION: Virulence factor that eliminates N-myristoyl protein
CC modifications in infected host cells. Acts as a cysteine protease that
CC cleaves the peptide bond between N-myristoylated Gly-2 and Asn-3 of
CC human ARF1, leading to the elimination of the myristoyl group and
CC alteration of protein trafficking in host cell. Could also cleave an
CC array of N-myristoylated host proteins involved in cellular growth,
CC signal transduction, autophagasome maturation and organelle function.
CC {ECO:0000269|PubMed:23535599}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18208325}. Host
CC cytoplasm {ECO:0000305|PubMed:18208325}. Note=Secreted via Mxi-Spa type
CC III secretion system (TTSS), and delivered into the host cytoplasm.
CC {ECO:0000305}.
CC -!- INDUCTION: Expression is temperature-independent.
CC {ECO:0000269|PubMed:9441862}.
CC -!- DISRUPTION PHENOTYPE: Mutants are not compromised in their ability to
CC invade cultured epithelial cells or to form plaques on BHK cell
CC monolayers. {ECO:0000269|PubMed:9441862}.
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DR EMBL; U32973; AAA84386.1; -; Genomic_DNA.
DR EMBL; AL391753; CAC05797.1; -; Genomic_DNA.
DR EMBL; AF348706; AAK18440.1; -; Genomic_DNA.
DR EMBL; AY206439; AAP78985.1; -; Genomic_DNA.
DR EMBL; AF386526; AAL72344.2; -; Genomic_DNA.
DR RefSeq; NP_085284.1; NC_002698.1.
DR RefSeq; NP_858255.2; NC_004851.1.
DR RefSeq; WP_005059304.1; NZ_WPGS01000043.1.
DR RefSeq; YP_009062479.1; NC_024996.1.
DR AlphaFoldDB; Q54150; -.
DR STRING; 198214.CP0122; -.
DR EnsemblBacteria; AAL72344; AAL72344; SF_p0122.
DR GeneID; 3170828; -.
DR KEGG; sfl:CP0122; -.
DR PATRIC; fig|198214.7.peg.5377; -.
DR HOGENOM; CLU_1146568_0_0_6; -.
DR OMA; NPRTHKD; -.
DR Proteomes; UP000001006; Plasmid pCP301.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Host cytoplasm; Hydrolase; Plasmid; Protease; Reference proteome; Secreted;
KW Virulence.
FT CHAIN 1..259
FT /note="Cysteine protease IpaJ"
FT /id="PRO_0000423395"
FT ACT_SITE 64
FT /evidence="ECO:0000305|PubMed:23535599"
FT ACT_SITE 206
FT /evidence="ECO:0000305|PubMed:23535599"
FT ACT_SITE 218
FT /evidence="ECO:0000305|PubMed:23535599"
FT MUTAGEN 64
FT /note="C->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:23535599"
FT MUTAGEN 206
FT /note="H->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:23535599"
FT MUTAGEN 218
FT /note="D->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:23535599"
SQ SEQUENCE 259 AA; 28807 MW; CB895A1FBB926353 CRC64;
MSEQRKPCKR GCIHTGVMLY GVLLQGAIPR EYMISHQTDV RVNENRVNEQ GCFLARKQMY
DNSCGAASLL CAAKELGVDK IPQYKGSMSE MTRKSSLDLD NRCERDLYLI TSGNYNPRIH
KDNIADAGYS MPDKIVMATR LLGLNAYVVE ESNIFSQVIS FIYPDARDLL IGMGCNIVHQ
RDVLSSNQRV LEAVAVSFIG VPVGLHWVLC RPDGSYMDPA VGENYSCFST MELGARRSNS
NFIGYTKIGI SIVITNEAL
