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Protein

Invasin IpaA

Gene

ipaA

Organism
Shigella flexneri
Status
Reviewed-Annotation score: -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

  • actin binding Source: UniProtKB-KW
  • vinculin binding Source: UniProtKB

GO - Biological processi

  • pathogenesis Source: UniProtKB-KW
  • positive regulation of actin filament depolymerization Source: UniProtKB

Keywordsi

Molecular functionActin-binding
Biological processVirulence

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
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

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)DescriptionActionsGraphical viewLength
ChainiPRO_00002214481 – 633Invasin IpaAAdd BLAST633

Proteomic databases

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 Homo sapiens.

GO - Molecular functioni

  • actin binding Source: UniProtKB-KW
  • vinculin binding Source: UniProtKB

Protein-protein interaction databases

IntActiP18010, 1 interactor
MINTiP18010

Structurei

Secondary structure

1633
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi492 – 507Combined sources16
Helixi566 – 582Combined sources17
Helixi611 – 627Combined sources17
Helixi628 – 630Combined sources3

3D structure databases

ProteinModelPortaliP18010
SMRiP18010
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18010

Family & Domainsi

Sequence similaritiesi

Belongs to the SipA/IpaA family.Curated

Phylogenomic databases

eggNOGiENOG4105MH6 Bacteria
ENOG4111VCG LUCA
HOGENOMiHOG000126669
KOiK13284

Family and domain databases

Gene3Di1.10.4150.10, 1 hit
InterProiView protein in InterPro
IPR015138 SipA
IPR023225 SipA_chaperone-bd
PfamiView protein in Pfam
PF09052 SipA, 1 hit
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)DescriptionActionsGraphical viewLength
Natural varianti385V → A in plasmid pCP301. 1

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
WP_005063225.1, NZ_MSJZ02000181.1
YP_009062482.1, NC_024996.1

Genome annotation databases

EnsemblBacteriaiAAL72353; AAL72353; SF_p0125
GeneIDi1238056
876595
KEGGisfl:CP0125
PATRICifig|198214.7.peg.5380

Similar proteinsi

Entry informationi

Entry nameiIPAA_SHIFL
AccessioniPrimary (citable) accession number: P18010
Secondary accession number(s): Q8VSH8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: July 18, 2018
This is version 128 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Plasmid, Reference proteome

Documents

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

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