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Protein

Invasin IpaA

Gene

ipaA

Organism
Shigella flexneri
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Rapidly associates with the first 265 amino acids of vinculin after bacteria-cell contact. This interaction is critical for efficient Shigella uptake. IpaA acts as a potent activator of vinculin and increase its ability to interact with F-actin. The complex IpaA-vinculin induces F-actin depolymerization along with the occasional formation of actin filament bundles.2 Publications

GO - Molecular functioni

  • vinculin binding Source: UniProtKB

GO - Biological processi

  • pathogenesis Source: UniProtKB-KW
  • positive regulation of actin filament depolymerization Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Virulence

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Invasin IpaA
Alternative name(s):
70 kDa antigen
Gene namesi
Name:ipaA
Ordered Locus Names:CP0125
Encoded oniPlasmid pWR1004 Publications
Plasmid pCP3011 Publication
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
Proteomesi
  • UP000001006 Componenti: Plasmid pCP301

Subcellular locationi

  • Secreted

  • Note: Secreted through the specialized type-III secretion system Mxi/Spa from the bacterium through the cell cytosol.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

Cells are still able to induce low levels of internalization, but are impaired in their ability to enter epithelial cells.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 633633Invasin IpaAPRO_0000221448Add
BLAST

Proteomic databases

PaxDbiP18010.
PRIDEiP18010.

Expressioni

Inductioni

Synthesis of this immunogen is repressed at 30 degrees Celsius and restored at 37 degrees Celsius.

Interactioni

Subunit structurei

The association of the vinculin-IpaA complex with actin occurs via the F-actin binding domain located on the tail of vinculin.

Binary interactionsi

WithEntry#Exp.IntActNotes
VCLP182063EBI-7640410,EBI-716775From a different organism.

GO - Molecular functioni

  • vinculin binding Source: UniProtKB

Protein-protein interaction databases

IntActiP18010. 1 interaction.
MINTiMINT-6174234.
STRINGi198214.CP0125.

Structurei

Secondary structure

1
633
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi492 – 50716Combined sources
Helixi566 – 58217Combined sources
Helixi611 – 62717Combined sources
Helixi628 – 6303Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GDCX-ray2.74B623-630[»]
2GWWX-ray2.72B602-631[»]
2HSQX-ray3.97B565-587[»]
2IBFX-ray3.20B/D563-587[»]
3RF3X-ray1.61C/D488-512[»]
ProteinModelPortaliP18010.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18010.

Family & Domainsi

Sequence similaritiesi

Belongs to the SipA/IpaA family.Curated

Phylogenomic databases

eggNOGiENOG4105MH6. Bacteria.
ENOG4111VCG. LUCA.
HOGENOMiHOG000126669.
KOiK13284.
OrthoDBiEOG6R87B2.

Family and domain databases

InterProiIPR015138. SipA.
IPR023225. SipA_chaperone-bd.
[Graphical view]
PfamiPF09052. SipA. 1 hit.
[Graphical view]
SUPFAMiSSF140746. SSF140746. 1 hit.

Sequencei

Sequence statusi: Complete.

P18010-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHNVNNTQAP TFLYKATSPS STEYSELKSK ISDIHSSQTS LKTPASVSEK
60 70 80 90 100
ENFATSFNQK CLDFLFSSSG KEDVLRSIYS NSMNAYAKSE ILEFSNVLYS
110 120 130 140 150
LVHQNGLNFE NEKGLQKIVA QYSELIIKDK LSQDSAFGPW SAKNKKLHQL
160 170 180 190 200
RQNIEHRLAL LAQQHTSGEA LSLGQKLLNT EVSSFIKNNI LAELKLSNET
210 220 230 240 250
VSSLKLDDLV DAQAKLAFDS LRNQRKNTID SKGFGIGKLS RDLNTVAVFP
260 270 280 290 300
ELLRKVLNDI LEDIKDSHPI QDGLPTPPED MPDGGPTPGA NEKTSQPVIH
310 320 330 340 350
YHINNDNRTY DNRVFDNRVY DNSYHENPEN DAQSPTSQTN DLLSRNGNSL
360 370 380 390 400
LNPQRALVQK VTSVLPHSIS DTVQTFANNS ALEKVFNHTP DNSDGIGSDL
410 420 430 440 450
LTTSSQERSA NNSLSRGHRP LNIQNSSTTP PLHPEGVTSS NDNSSDTTKS
460 470 480 490 500
SASLSHRVAS QINKFNSNTD SKVLQTDFLS RNGDTYLTRE TIFEASKKVT
510 520 530 540 550
NSLSNLISLI GTKSGTQERE LQEKSKDITK STTEHRINNK LKVTDANIRN
560 570 580 590 600
YVTETNADTI DKNHAIYEKA KEVSSALSKV LSKIDDTSAE LLTDDISDLK
610 620 630
NNNDITAENN NIYKAAKDVT TSLSKVLKNI NKD
Length:633
Mass (Da):70,093
Last modified:November 1, 1990 - v1
Checksum:i2F804F45355E4751
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti385 – 3851V → A in plasmid pCP301.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17628 Genomic DNA. Translation: CAA35624.1.
AL391753 Genomic DNA. Translation: CAC05800.1.
AF348706 Genomic DNA. Translation: AAK18443.1.
AF386526 Genomic DNA. Translation: AAL72353.1.
J04117 Genomic DNA. Translation: AAA26525.1.
PIRiS12763. E31265.
RefSeqiNP_085287.1. NC_002698.1.
NP_858258.1. NC_004851.1.
YP_009062482.1. NC_024996.1.

Genome annotation databases

EnsemblBacteriaiAAL72353; AAL72353; SF_p0125.
GeneIDi1238056.
876595.
KEGGipg:20467551.
pg:876595.
sfl:CP0125.
PATRICi18722579. VBIShiFle86970_5380.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17628 Genomic DNA. Translation: CAA35624.1.
AL391753 Genomic DNA. Translation: CAC05800.1.
AF348706 Genomic DNA. Translation: AAK18443.1.
AF386526 Genomic DNA. Translation: AAL72353.1.
J04117 Genomic DNA. Translation: AAA26525.1.
PIRiS12763. E31265.
RefSeqiNP_085287.1. NC_002698.1.
NP_858258.1. NC_004851.1.
YP_009062482.1. NC_024996.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GDCX-ray2.74B623-630[»]
2GWWX-ray2.72B602-631[»]
2HSQX-ray3.97B565-587[»]
2IBFX-ray3.20B/D563-587[»]
3RF3X-ray1.61C/D488-512[»]
ProteinModelPortaliP18010.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP18010. 1 interaction.
MINTiMINT-6174234.
STRINGi198214.CP0125.

Proteomic databases

PaxDbiP18010.
PRIDEiP18010.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL72353; AAL72353; SF_p0125.
GeneIDi1238056.
876595.
KEGGipg:20467551.
pg:876595.
sfl:CP0125.
PATRICi18722579. VBIShiFle86970_5380.

Phylogenomic databases

eggNOGiENOG4105MH6. Bacteria.
ENOG4111VCG. LUCA.
HOGENOMiHOG000126669.
KOiK13284.
OrthoDBiEOG6R87B2.

Miscellaneous databases

EvolutionaryTraceiP18010.

Family and domain databases

InterProiIPR015138. SipA.
IPR023225. SipA_chaperone-bd.
[Graphical view]
PfamiPF09052. SipA. 1 hit.
[Graphical view]
SUPFAMiSSF140746. SSF140746. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of invasion plasmid antigen gene ipaA from Shigella flexneri 5."
    Venkatesan M.M., Buysse J.M.
    Nucleic Acids Res. 18:1648-1648(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: M90T / Serotype 5a.
    Plasmid: pWR100
  2. "The virulence plasmid pWR100 and the repertoire of proteins secreted by the type III secretion apparatus of Shigella flexneri."
    Buchrieser C., Glaser P., Rusniok C., Nedjari H., d'Hauteville H., Kunst F., Sansonetti P.J., Parsot C.
    Mol. Microbiol. 38:760-771(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: M90T / Serotype 5a.
    Plasmid: pWR100
  3. "Complete DNA sequence and analysis of the large virulence plasmid of Shigella flexneri."
    Venkatesan M.M., Goldberg M.B., Rose D.J., Grotbeck E.J., Burland V., Blattner F.R.
    Infect. Immun. 69:3271-3285(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: M90T / Serotype 5a.
    Plasmid: pWR100
  4. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
    Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
    , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
    Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 301 / Serotype 2a.
    Plasmid: pCP301
  5. "Characterization of invasion plasmid antigen genes (ipaBCD) from Shigella flexneri."
    Venkatesan M.M., Buysse J.M., Kopecko D.J.
    Proc. Natl. Acad. Sci. U.S.A. 85:9317-9321(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-88.
    Strain: M90T / Serotype 5a.
    Plasmid: pWR100
  6. "Modulation of bacterial entry into epithelial cells by association between vinculin and the Shigella IpaA invasin."
    Tran Van Nhieu G., Ben-Ze'ev A., Sansonetti P.J.
    EMBO J. 16:2717-2729(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. "Binding of the Shigella protein IpaA to vinculin induces F-actin depolymerization."
    Bourdet-Sicard R., Ruediger M., Jockusch B.M., Gounon P., Sansonetti P.J., Tran Van Nhieu G.
    EMBO J. 18:5853-5862(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiIPAA_SHIFL
AccessioniPrimary (citable) accession number: P18010
Secondary accession number(s): Q8VSH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: May 11, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.