ID   IPAD_SHIDY              Reviewed;         332 AA.
AC   Q03947;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Invasin IpaD;
DE   AltName: Full=37 kDa membrane antigen;
GN   Name=ipaD;
OS   Shigella dysenteriae.
OG   Plasmid Invasion.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=622;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CG097;
RX   PubMed=1766387; DOI=10.1111/j.1365-2958.1991.tb02151.x;
RA   Yao R., Palchaudhuri S.;
RT   "Nucleotide sequence of the ipaBCD structural genes of Shigella
RT   dysenteriae.";
RL   Mol. Microbiol. 5:2217-2221(1991).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted via the
CC       type III secretion system (TTSS). Localizes to the tip of the external
CC       secretion needle that is part of the TTSS apparatus (By similarity).
CC       {ECO:0000250}.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the invasin protein D family. {ECO:0000305}.
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DR   EMBL; X60777; CAA43192.1; -; Genomic_DNA.
DR   PIR; S15579; S15579.
DR   AlphaFoldDB; Q03947; -.
DR   SMR; Q03947; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
KW   Coiled coil; Plasmid; Secreted; Virulence.
FT   CHAIN           1..332
FT                   /note="Invasin IpaD"
FT                   /id="PRO_0000219861"
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:0000250"
FT   COILED          44..77
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   332 AA;  36598 MW;  916FEA4B394E9046 CRC64;
     MNITTLTNSI STSSFSPNNT NGSSTETVNS DIKTTTSSHP VSSLTMLNDT LHNIRTTNQA
     LKKELSQKTL TKTSLEEIAL HSSQISMDVN KSAQLLNILS KTEYPINKDA RELLHSAPKE
     AELDGYEMIS HRELWAKIAN SINDINEQYL KVYEHAVSSY TQMYQEFSAV LSSLAGWISP
     GGNDGNSVKL QVKSLKDALT TLKKNYEDKP LYPATNTVSE QEANKWLTEL GGTIGTVSAK
     NGGYVVSINM TPIYNMLNRL DNLGGNGEVV LDNAKYQAWN AGFSAEDETM KNNLQTLVQK
     YSNANSIFDN LVKVLSSTIS SCTDTDKLFL HF