IPAD_SHIFL
ID IPAD_SHIFL Reviewed; 332 AA.
AC P18013; Q6XVZ1;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Invasin IpaD;
DE AltName: Full=36 kDa membrane antigen;
GN Name=ipaD; OrderedLocusNames=CP0126;
OS Shigella flexneri.
OG Plasmid pWR100, Plasmid pMYSH6000, Plasmid pINV_F6_M1382, and
OG Plasmid pCP301.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=3057506; DOI=10.1073/pnas.85.23.9317;
RA Venkatesan M.M., Buysse J.M., Kopecko D.J.;
RT "Characterization of invasion plasmid antigen genes (ipaBCD) from Shigella
RT flexneri.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:9317-9321(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=YSH6000 / Serotype 2a; PLASMID=pMYSH6000;
RX PubMed=2552264; DOI=10.1111/j.1365-2958.1989.tb00269.x;
RA Sasakawa C., Adler B., Tobe T., Okada N., Nagai S., Komatsu K.,
RA Yoshikawa M.;
RT "Functional organization and nucleotide sequence of virulence region-2 on
RT the large virulence plasmid in Shigella flexneri 2a.";
RL Mol. Microbiol. 3:1191-1201(1989).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-259.
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=3071655; DOI=10.1016/0882-4010(88)90062-9;
RA Baudry B., Kaczorek M., Sansonetti P.J.;
RT "Nucleotide sequence of the invasion plasmid antigen B and C genes (ipaB
RT and ipaC) of Shigella flexneri.";
RL Microb. Pathog. 4:345-357(1988).
RN [8]
RP FUNCTION.
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=7957095; DOI=10.1002/j.1460-2075.1994.tb06863.x;
RA Menard R., Sansonetti P., Parsot C.;
RT "The secretion of the Shigella flexneri Ipa invasins is activated by
RT epithelial cells and controlled by IpaB and IpaD.";
RL EMBO J. 13:5293-5302(1994).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF 321-SER-CYS-322.
RC STRAIN=M90T / Serotype 5a; PLASMID=pWR100;
RX PubMed=15731041; DOI=10.1128/iai.73.3.1432-1440.2005;
RA Picking W.L., Nishioka H., Hearn P.D., Baxter M.A., Harrington A.T.,
RA Blocker A., Picking W.D.;
RT "IpaD of Shigella flexneri is independently required for regulation of Ipa
RT protein secretion and efficient insertion of IpaB and IpaC into host
RT membranes.";
RL Infect. Immun. 73:1432-1440(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 15-332, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF LYS-151 AND GLU-154.
RX PubMed=17077085; DOI=10.1074/jbc.m607945200;
RA Johnson S., Roversi P., Espina M., Olive A., Deane J.E., Birket S.,
RA Field T., Picking W.D., Blocker A.J., Galyov E.E., Picking W.L., Lea S.M.;
RT "Self-chaperoning of the type III secretion system needle tip proteins IpaD
RT and BipD.";
RL J. Biol. Chem. 282:4035-4044(2007).
CC -!- FUNCTION: Required for bacterial invasion of host cells. Controls IpaB
CC and IpaC secretion, and the efficiency with which they are physically
CC inserted into target cell membranes. These proteins are exported via
CC TTSS to form a pore in the host membrane that allows the translocation
CC of the other effectors into the host cytoplasm. Along with IpaB, is
CC essential for both blocking secretion through the Mxi/Spa translocon in
CC the absence of a secretion-inducing signal, and for controlling the
CC level of secretion in the presence of this signal.
CC {ECO:0000269|PubMed:15731041, ECO:0000269|PubMed:7957095}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17077085}.
CC Note=Secreted via the type III secretion system (TTSS). Localizes to
CC the tip of the external secretion needle that is part of the TTSS
CC apparatus.
CC -!- INDUCTION: Synthesis of this immunogen is repressed at 30 degrees
CC Celsius and restored at 37 degrees Celsius.
CC -!- DOMAIN: The N-terminal domain is an intra-molecular chaperone that
CC prevents premature oligomerization of the residues on the coiled-coil
CC region that are involved in interactions with the needle and/or itself.
CC The residues in the C-terminal domain probably form oligomeric
CC structures at the tip of the needle that are responsible for the
CC regulation of secretion of other effectors.
CC -!- MISCELLANEOUS: Deletion of amino acids 1-20 abolishes invasion
CC activity, affects contact-mediated hemolysis activity and IpaD
CC secretion. Deletion of amino acids 41-80 and 81-120 restores invasion
CC activity to a higher level than wild-type and reduces contact-mediated
CC hemolysis activity. Deletion beyond amino acid 120 reduces invasion
CC activity and abolishes contact-mediated hemolysis activity.
CC -!- SIMILARITY: Belongs to the invasin protein D family. {ECO:0000305}.
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DR EMBL; J04117; AAA26524.1; -; Genomic_DNA.
DR EMBL; X15319; CAA33383.1; -; Genomic_DNA.
DR EMBL; AL391753; CAC05801.1; -; Genomic_DNA.
DR EMBL; AF348706; AAK18444.1; -; Genomic_DNA.
DR EMBL; AY206439; AAP78989.1; -; Genomic_DNA.
DR EMBL; AF386526; AAL72350.1; -; Genomic_DNA.
DR EMBL; M34849; AAA98426.1; -; Genomic_DNA.
DR PIR; D31265; D31265.
DR RefSeq; NP_085288.1; NC_002698.1.
DR RefSeq; NP_858259.1; NC_004851.1.
DR RefSeq; WP_010921661.1; NZ_QWST01000007.1.
DR RefSeq; YP_009062483.1; NC_024996.1.
DR PDB; 2J0N; X-ray; 2.10 A; A/B=133-332.
DR PDB; 2J0O; X-ray; 3.00 A; A/B=15-332.
DR PDB; 2JAA; X-ray; 3.10 A; A/B=121-332.
DR PDB; 3R9V; X-ray; 1.90 A; A/B=39-322.
DR PDB; 4D3E; EM; 2.12 A; D=125-332.
DR PDB; 5VXJ; X-ray; 2.50 A; A/C/E/G/I=38-322.
DR PDB; 5VXK; X-ray; 2.55 A; A=39-322.
DR PDB; 5VXL; X-ray; 2.80 A; A=39-322.
DR PDB; 5VXM; X-ray; 2.05 A; A=39-322.
DR PDBsum; 2J0N; -.
DR PDBsum; 2J0O; -.
DR PDBsum; 2JAA; -.
DR PDBsum; 3R9V; -.
DR PDBsum; 4D3E; -.
DR PDBsum; 5VXJ; -.
DR PDBsum; 5VXK; -.
DR PDBsum; 5VXL; -.
DR PDBsum; 5VXM; -.
DR AlphaFoldDB; P18013; -.
DR SMR; P18013; -.
DR STRING; 198214.CP0126; -.
DR TCDB; 1.C.36.3.1; the bacterial type iii-target cell pore (iiitcp) family.
DR PRIDE; P18013; -.
DR ABCD; P18013; 4 sequenced antibodies.
DR EnsemblBacteria; AAL72350; AAL72350; SF_p0126.
DR GeneID; 1238053; -.
DR KEGG; sfl:CP0126; -.
DR PATRIC; fig|198214.7.peg.5381; -.
DR HOGENOM; CLU_069613_0_0_6; -.
DR EvolutionaryTrace; P18013; -.
DR PHI-base; PHI:7721; -.
DR Proteomes; UP000001006; Plasmid pCP301.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0034055; P:effector-mediated induction of programmed cell death in host; IDA:CACAO.
DR Gene3D; 1.20.1710.10; -; 1.
DR InterPro; IPR036708; BipD-like_sf.
DR InterPro; IPR009483; IpaD.
DR Pfam; PF06511; T3SS_TC; 1.
DR SUPFAM; SSF140693; SSF140693; 1.
DR TIGRFAMs; TIGR02553; SipD_IpaD_SspD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Plasmid; Reference proteome; Secreted;
KW Virulence.
FT CHAIN 1..332
FT /note="Invasin IpaD"
FT /id="PRO_0000219862"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..267
FT /note="IpaB binding"
FT /evidence="ECO:0000305"
FT COILED 44..77
FT /evidence="ECO:0000255"
FT VARIANT 64
FT /note="E -> D (in plasmid pINV_F6_M1382)"
FT VARIANT 101..102
FT /note="RN -> KK (in plasmid pINV_F6_M1382)"
FT VARIANT 102
FT /note="N -> H (in plasmid pMYSH6000 and plasmid pCP301)"
FT VARIANT 126..127
FT /note="DQ -> YE (in plasmid pINV_F6_M1382)"
FT VARIANT 136
FT /note="A -> D (in plasmid pINV_F6_M1382)"
FT VARIANT 140
FT /note="N -> K (in plasmid pINV_F6_M1382)"
FT VARIANT 144
FT /note="D -> N (in plasmid pINV_F6_M1382)"
FT VARIANT 193
FT /note="N -> K (in plasmid pINV_F6_M1382)"
FT VARIANT 197..201
FT /note="KALEE -> DELTK (in plasmid pINV_F6_M1382)"
FT VARIANT 220
FT /note="Q -> K (in plasmid pINV_F6_M1382)"
FT VARIANT 239
FT /note="Q -> E (in plasmid pINV_F6_M1382)"
FT VARIANT 247
FT /note="S -> N (in plasmid pINV_F6_M1382)"
FT MUTAGEN 151
FT /note="K->E: 50% reduction in hemolytic activity; when
FT associated with K-154."
FT /evidence="ECO:0000269|PubMed:17077085"
FT MUTAGEN 154
FT /note="E->K: 50% reduction in hemolytic activity; when
FT associated with E-151."
FT /evidence="ECO:0000269|PubMed:17077085"
FT MUTAGEN 321..322
FT /note="SC->AS: Restores invasion activity in a nonpolar
FT ipaD mutant."
FT /evidence="ECO:0000269|PubMed:15731041"
FT HELIX 43..65
FT /evidence="ECO:0007829|PDB:5VXM"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:5VXM"
FT HELIX 72..95
FT /evidence="ECO:0007829|PDB:5VXM"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:5VXM"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:5VXJ"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:3R9V"
FT HELIX 131..148
FT /evidence="ECO:0007829|PDB:3R9V"
FT HELIX 150..174
FT /evidence="ECO:0007829|PDB:3R9V"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:3R9V"
FT STRAND 178..190
FT /evidence="ECO:0007829|PDB:3R9V"
FT HELIX 192..206
FT /evidence="ECO:0007829|PDB:3R9V"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:2J0O"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:3R9V"
FT HELIX 220..230
FT /evidence="ECO:0007829|PDB:3R9V"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:3R9V"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:3R9V"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:3R9V"
FT HELIX 251..262
FT /evidence="ECO:0007829|PDB:3R9V"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:3R9V"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:3R9V"
FT HELIX 273..317
FT /evidence="ECO:0007829|PDB:3R9V"
SQ SEQUENCE 332 AA; 36639 MW; C646F75AA946B782 CRC64;
MNITTLTNSI STSSFSPNNT NGSSTETVNS DIKTTTSSHP VSSLTMLNDT LHNIRTTNQA
LKKELSQKTL TKTSLEEIAL HSSQISMDVN KSAQLLDILS RNEYPINKDA RELLHSAPKE
AELDGDQMIS HRELWAKIAN SINDINEQYL KVYEHAVSSY TQMYQDFSAV LSSLAGWISP
GGNDGNSVKL QVNSLKKALE ELKEKYKDKP LYPANNTVSQ EQANKWLTEL GGTIGKVSQK
NGGYVVSINM TPIDNMLKSL DNLGGNGEVV LDNAKYQAWN AGFSAEDETM KNNLQTLVQK
YSNANSIFDN LVKVLSSTIS SCTDTDKLFL HF
