IPAA_SHIFL
ID IPAA_SHIFL Reviewed; 633 AA.
AC P18010; Q8VSH8;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Invasin IpaA;
DE AltName: Full=70 kDa antigen;
GN Name=ipaA; OrderedLocusNames=CP0125;
OS Shigella flexneri.
OG Plasmid pWR100, and 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=2183200; DOI=10.1093/nar/18.6.1648;
RA Venkatesan M.M., Buysse J.M.;
RT "Nucleotide sequence of invasion plasmid antigen gene ipaA from Shigella
RT flexneri 5.";
RL Nucleic Acids Res. 18:1648-1648(1990).
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 [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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-88.
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9184218; DOI=10.1093/emboj/16.10.2717;
RA Tran Van Nhieu G., Ben-Ze'ev A., Sansonetti P.J.;
RT "Modulation of bacterial entry into epithelial cells by association between
RT vinculin and the Shigella IpaA invasin.";
RL EMBO J. 16:2717-2729(1997).
RN [7]
RP FUNCTION.
RX PubMed=10545097; DOI=10.1093/emboj/18.21.5853;
RA Bourdet-Sicard R., Ruediger M., Jockusch B.M., Gounon P., Sansonetti P.J.,
RA Tran Van Nhieu G.;
RT "Binding of the Shigella protein IpaA to vinculin induces F-actin
RT depolymerization.";
RL EMBO J. 18:5853-5862(1999).
CC -!- FUNCTION: Rapidly associates with the first 265 amino acids of vinculin
CC after bacteria-cell contact. This interaction is critical for efficient
CC Shigella uptake. IpaA acts as a potent activator of vinculin and
CC increase its ability to interact with F-actin. The complex IpaA-
CC vinculin induces F-actin depolymerization along with the occasional
CC formation of actin filament bundles. {ECO:0000269|PubMed:10545097,
CC ECO:0000269|PubMed:9184218}.
CC -!- SUBUNIT: The association of the vinculin-IpaA complex with actin occurs
CC via the F-actin binding domain located on the tail of vinculin.
CC -!- INTERACTION:
CC P18010; P18206: VCL; Xeno; NbExp=7; IntAct=EBI-7640410, EBI-716775;
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted through the specialized
CC type-III secretion system Mxi/Spa from the bacterium through the cell
CC cytosol.
CC -!- INDUCTION: Synthesis of this immunogen is repressed at 30 degrees
CC Celsius and restored at 37 degrees Celsius.
CC -!- DISRUPTION PHENOTYPE: Cells are still able to induce low levels of
CC internalization, but are impaired in their ability to enter epithelial
CC cells. {ECO:0000269|PubMed:9184218}.
CC -!- SIMILARITY: Belongs to the SipA/IpaA family. {ECO:0000305}.
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DR EMBL; X17628; CAA35624.1; -; Genomic_DNA.
DR EMBL; AL391753; CAC05800.1; -; Genomic_DNA.
DR EMBL; AF348706; AAK18443.1; -; Genomic_DNA.
DR EMBL; AF386526; AAL72353.1; -; Genomic_DNA.
DR EMBL; J04117; AAA26525.1; -; Genomic_DNA.
DR PIR; S12763; E31265.
DR RefSeq; NP_085287.1; NC_002698.1.
DR RefSeq; NP_858258.1; NC_004851.1.
DR RefSeq; WP_005063225.1; NZ_UIPM01000036.1.
DR RefSeq; YP_009062482.1; NC_024996.1.
DR PDB; 2GDC; X-ray; 2.74 A; B=623-630.
DR PDB; 2GWW; X-ray; 2.72 A; B=602-631.
DR PDB; 2HSQ; X-ray; 3.97 A; B=565-587.
DR PDB; 2IBF; X-ray; 3.20 A; B/D=563-587.
DR PDB; 3RF3; X-ray; 1.61 A; C/D=488-512.
DR PDB; 5NL1; X-ray; 2.50 A; G/H/I/J/K/L=488-512.
DR PDBsum; 2GDC; -.
DR PDBsum; 2GWW; -.
DR PDBsum; 2HSQ; -.
DR PDBsum; 2IBF; -.
DR PDBsum; 3RF3; -.
DR PDBsum; 5NL1; -.
DR AlphaFoldDB; P18010; -.
DR SMR; P18010; -.
DR IntAct; P18010; 1.
DR MINT; P18010; -.
DR STRING; 198214.CP0125; -.
DR PRIDE; P18010; -.
DR EnsemblBacteria; AAL72353; AAL72353; SF_p0125.
DR GeneID; 1238056; -.
DR KEGG; sfl:CP0125; -.
DR PATRIC; fig|198214.7.peg.5380; -.
DR HOGENOM; CLU_432046_0_0_6; -.
DR EvolutionaryTrace; P18010; -.
DR Proteomes; UP000001006; Plasmid pCP301.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0017166; F:vinculin binding; IPI:UniProtKB.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; IDA:UniProtKB.
DR Gene3D; 1.10.4150.10; -; 1.
DR InterPro; IPR023225; SipA_chaperone-bd.
DR InterPro; IPR015138; SipA_N.
DR InterPro; IPR040658; SipA_VBS.
DR Pfam; PF09052; SipA; 1.
DR Pfam; PF17985; SipA_VBS; 3.
DR SUPFAM; SSF140746; SSF140746; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Plasmid; Reference proteome; Secreted;
KW Virulence.
FT CHAIN 1..633
FT /note="Invasin IpaA"
FT /id="PRO_0000221448"
FT REGION 267..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 385
FT /note="V -> A (in plasmid pCP301)"
FT HELIX 492..507
FT /evidence="ECO:0007829|PDB:3RF3"
FT HELIX 566..582
FT /evidence="ECO:0007829|PDB:2IBF"
FT HELIX 611..627
FT /evidence="ECO:0007829|PDB:2GWW"
FT HELIX 628..630
FT /evidence="ECO:0007829|PDB:2GWW"
SQ SEQUENCE 633 AA; 70093 MW; 2F804F45355E4751 CRC64;
MHNVNNTQAP TFLYKATSPS STEYSELKSK ISDIHSSQTS LKTPASVSEK ENFATSFNQK
CLDFLFSSSG KEDVLRSIYS NSMNAYAKSE ILEFSNVLYS LVHQNGLNFE NEKGLQKIVA
QYSELIIKDK LSQDSAFGPW SAKNKKLHQL RQNIEHRLAL LAQQHTSGEA LSLGQKLLNT
EVSSFIKNNI LAELKLSNET VSSLKLDDLV DAQAKLAFDS LRNQRKNTID SKGFGIGKLS
RDLNTVAVFP ELLRKVLNDI LEDIKDSHPI QDGLPTPPED MPDGGPTPGA NEKTSQPVIH
YHINNDNRTY DNRVFDNRVY DNSYHENPEN DAQSPTSQTN DLLSRNGNSL LNPQRALVQK
VTSVLPHSIS DTVQTFANNS ALEKVFNHTP DNSDGIGSDL LTTSSQERSA NNSLSRGHRP
LNIQNSSTTP PLHPEGVTSS NDNSSDTTKS SASLSHRVAS QINKFNSNTD SKVLQTDFLS
RNGDTYLTRE TIFEASKKVT NSLSNLISLI GTKSGTQERE LQEKSKDITK STTEHRINNK
LKVTDANIRN YVTETNADTI DKNHAIYEKA KEVSSALSKV LSKIDDTSAE LLTDDISDLK
NNNDITAENN NIYKAAKDVT TSLSKVLKNI NKD
