UniProtKB - P18010 (IPAA_SHIFL)
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Protein
Invasin IpaA
Gene
ipaA
Organism
Shigella flexneri
Status
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 function | Actin-binding |
| Biological process | Virulence |
Names & Taxonomyi
| Protein namesi | Recommended name: Invasin IpaAAlternative name(s): 70 kDa antigen |
| Gene namesi | Name:ipaA Ordered Locus Names:CP0125 |
| Encoded oni | Plasmid pWR1004 Publications Plasmid pCP3011 Publication |
| Organismi | Shigella flexneri |
| Taxonomic identifieri | 623 [NCBI] |
| Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Shigella |
| Proteomesi |
|
Subcellular locationi
- Secreted
Note: Secreted through the specialized type-III secretion system Mxi/Spa from the bacterium through the cell cytosol.
GO - Cellular componenti
- extracellular region Source: UniProtKB-SubCell
Keywords - Cellular componenti
SecretedPathology & 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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| ChainiPRO_0000221448 | 1 – 633 | Invasin IpaAAdd BLAST | 633 |
Proteomic databases
| PaxDbi | P18010. |
| PRIDEi | P18010. |
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
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| VCL | P18206 | 3 | EBI-7640410,EBI-716775 | From Homo sapiens. |
GO - Molecular functioni
- actin binding Source: UniProtKB-KW
- vinculin binding Source: UniProtKB
Protein-protein interaction databases
| IntActi | P18010. 1 interactor. |
| MINTi | MINT-6174234. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Helixi | 492 – 507 | Combined sources | 16 | |
| Helixi | 566 – 582 | Combined sources | 17 | |
| Helixi | 611 – 627 | Combined sources | 17 | |
| Helixi | 628 – 630 | Combined sources | 3 |
3D structure databases
| Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 2GDC | X-ray | 2.74 | B | 623-630 | [»] | |
| 2GWW | X-ray | 2.72 | B | 602-631 | [»] | |
| 2HSQ | X-ray | 3.97 | B | 565-587 | [»] | |
| 2IBF | X-ray | 3.20 | B/D | 563-587 | [»] | |
| 3RF3 | X-ray | 1.61 | C/D | 488-512 | [»] | |
| ProteinModelPortali | P18010. | |||||
| SMRi | P18010. | |||||
| ModBasei | Search... | |||||
| MobiDBi | Search... | |||||
Miscellaneous databases
| EvolutionaryTracei | P18010. |
Family & Domainsi
Sequence similaritiesi
Belongs to the SipA/IpaA family.Curated
Phylogenomic databases
| eggNOGi | ENOG4105MH6. Bacteria. ENOG4111VCG. LUCA. |
| HOGENOMi | HOG000126669. |
| KOi | K13284. |
Family and domain databases
| Gene3Di | 1.10.4150.10. 1 hit. |
| InterProi | View protein in InterPro IPR015138. SipA. IPR023225. SipA_chaperone-bd. |
| Pfami | View protein in Pfam PF09052. SipA. 1 hit. |
| SUPFAMi | SSF140746. SSF140746. 1 hit. |
Sequencei
Sequence statusi: Complete.
P18010-1 [UniParc]FASTAAdd to basket
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
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Natural varianti | 385 | V → 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. |
| PIRi | S12763. E31265. |
| RefSeqi | NP_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
| EnsemblBacteriai | AAL72353; AAL72353; SF_p0125. |
| GeneIDi | 1238056. 876595. |
| KEGGi | sfl:CP0125. |
| PATRICi | fig|198214.7.peg.5380. |
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. |
Entry informationi
| Entry namei | IPAA_SHIFL | |
| Accessioni | P18010Primary (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: | July 5, 2017 | |
| This is version 122 of the entry and version 1 of the sequence. See complete history. | ||
| Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Prokaryotic Protein Annotation Program | |
Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, PlasmidDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
