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Protein

Invasin IpaD

Gene

ipaD

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

Functioni

Required for bacterial invasion of host cells. Controls IpaB and IpaC secretion, and the efficiency with which they are physically inserted into target cell membranes. These proteins are exported via TTSS to form a pore in the host membrane that allows the translocation of the other effectors into the host cytoplasm. Along with IpaB, is essential for both blocking secretion through the Mxi/Spa translocon in the absence of a secretion-inducing signal, and for controlling the level of secretion in the presence of this signal.2 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Virulence

Protein family/group databases

TCDBi1.C.36.3.1. the bacterial type iii-target cell pore (iiitcp) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Invasin IpaD
Alternative name(s):
36 kDa membrane antigen
Gene namesi
Name:ipaD
Ordered Locus Names:CP0126
Encoded oniPlasmid pWR1006 Publications
Plasmid pMYSH60001 Publication
Plasmid pINV_F6_M13821 Publication
Plasmid pCP3011 Publication
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
Proteomesi
  • UP000001006 Componenti: Plasmid pCP301

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi151 – 1511K → E: 50% reduction in hemolytic activity; when associated with K-154. 1 Publication
Mutagenesisi154 – 1541E → K: 50% reduction in hemolytic activity; when associated with E-151. 1 Publication
Mutagenesisi321 – 3222SC → AS: Restores invasion activity in a nonpolar ipaD mutant. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 332332Invasin IpaDPRO_0000219862Add
BLAST

Proteomic databases

PaxDbiP18013.

Expressioni

Inductioni

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

Interactioni

Protein-protein interaction databases

STRINGi198214.CP0126.

Structurei

Secondary structure

1
332
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 6526Combined sources
Helixi72 – 10130Combined sources
Helixi108 – 1125Combined sources
Helixi113 – 1164Combined sources
Turni119 – 1213Combined sources
Beta strandi128 – 1303Combined sources
Helixi131 – 14818Combined sources
Helixi150 – 17425Combined sources
Helixi175 – 1773Combined sources
Beta strandi178 – 19013Combined sources
Helixi192 – 20615Combined sources
Beta strandi210 – 2134Combined sources
Beta strandi214 – 2163Combined sources
Helixi220 – 23011Combined sources
Turni232 – 2343Combined sources
Beta strandi235 – 2395Combined sources
Beta strandi241 – 2488Combined sources
Helixi251 – 26212Combined sources
Beta strandi265 – 2673Combined sources
Beta strandi269 – 2713Combined sources
Helixi273 – 31745Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J0NX-ray2.10A/B133-332[»]
2J0OX-ray3.00A/B15-332[»]
2JAAX-ray3.10A/B121-332[»]
3R9VX-ray1.90A/B39-322[»]
4D3Eelectron microscopy2.12D125-332[»]
ProteinModelPortaliP18013.
SMRiP18013. Positions 39-322.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18013.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni192 – 26776IpaB bindingCuratedAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili44 – 7734Sequence analysisAdd
BLAST

Domaini

The N-terminal domain is an intra-molecular chaperone that prevents premature oligomerization of the residues on the coiled-coil region that are involved in interactions with the needle and/or itself. The residues in the C-terminal domain probably form oligomeric structures at the tip of the needle that are responsible for the regulation of secretion of other effectors.

Sequence similaritiesi

Belongs to the invasin protein D family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG4105IBT. Bacteria.
ENOG4111P3X. LUCA.
HOGENOMiHOG000012181.
KOiK13287.

Family and domain databases

InterProiIPR009483. Plasmid_invsIpaD.
IPR013386. T3SS_IpaD/SipD/SspD.
[Graphical view]
PfamiPF06511. IpaD. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02553. SipD_IpaD_SspD. 1 hit.

Sequencei

Sequence statusi: Complete.

P18013-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNITTLTNSI STSSFSPNNT NGSSTETVNS DIKTTTSSHP VSSLTMLNDT
60 70 80 90 100
LHNIRTTNQA LKKELSQKTL TKTSLEEIAL HSSQISMDVN KSAQLLDILS
110 120 130 140 150
RNEYPINKDA RELLHSAPKE AELDGDQMIS HRELWAKIAN SINDINEQYL
160 170 180 190 200
KVYEHAVSSY TQMYQDFSAV LSSLAGWISP GGNDGNSVKL QVNSLKKALE
210 220 230 240 250
ELKEKYKDKP LYPANNTVSQ EQANKWLTEL GGTIGKVSQK NGGYVVSINM
260 270 280 290 300
TPIDNMLKSL DNLGGNGEVV LDNAKYQAWN AGFSAEDETM KNNLQTLVQK
310 320 330
YSNANSIFDN LVKVLSSTIS SCTDTDKLFL HF
Length:332
Mass (Da):36,639
Last modified:November 1, 1990 - v1
Checksum:iC646F75AA946B782
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti64 – 641E → D in plasmid pINV_F6_M1382.
Natural varianti101 – 1022RN → KK in plasmid pINV_F6_M1382.
Natural varianti102 – 1021N → H in plasmid pMYSH6000 and plasmid pCP301.
Natural varianti126 – 1272DQ → YE in plasmid pINV_F6_M1382.
Natural varianti136 – 1361A → D in plasmid pINV_F6_M1382.
Natural varianti140 – 1401N → K in plasmid pINV_F6_M1382.
Natural varianti144 – 1441D → N in plasmid pINV_F6_M1382.
Natural varianti193 – 1931N → K in plasmid pINV_F6_M1382.
Natural varianti197 – 2015KALEE → DELTK in plasmid pINV_F6_M1382.
Natural varianti220 – 2201Q → K in plasmid pINV_F6_M1382.
Natural varianti239 – 2391Q → E in plasmid pINV_F6_M1382.
Natural varianti247 – 2471S → N in plasmid pINV_F6_M1382.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04117 Genomic DNA. Translation: AAA26524.1.
X15319 Genomic DNA. Translation: CAA33383.1.
AL391753 Genomic DNA. Translation: CAC05801.1.
AF348706 Genomic DNA. Translation: AAK18444.1.
AY206439 Genomic DNA. Translation: AAP78989.1.
AF386526 Genomic DNA. Translation: AAL72350.1.
M34849 Genomic DNA. Translation: AAA98426.1.
PIRiD31265.
RefSeqiNP_085288.1. NC_002698.1.
NP_858259.1. NC_004851.1.
YP_009062483.1. NC_024996.1.

Genome annotation databases

EnsemblBacteriaiAAL72350; AAL72350; SF_p0126.
GeneIDi876444.
KEGGipg:20467558.
pg:876444.
sfl:CP0126.
PATRICi18722581. VBIShiFle86970_5381.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04117 Genomic DNA. Translation: AAA26524.1.
X15319 Genomic DNA. Translation: CAA33383.1.
AL391753 Genomic DNA. Translation: CAC05801.1.
AF348706 Genomic DNA. Translation: AAK18444.1.
AY206439 Genomic DNA. Translation: AAP78989.1.
AF386526 Genomic DNA. Translation: AAL72350.1.
M34849 Genomic DNA. Translation: AAA98426.1.
PIRiD31265.
RefSeqiNP_085288.1. NC_002698.1.
NP_858259.1. NC_004851.1.
YP_009062483.1. NC_024996.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J0NX-ray2.10A/B133-332[»]
2J0OX-ray3.00A/B15-332[»]
2JAAX-ray3.10A/B121-332[»]
3R9VX-ray1.90A/B39-322[»]
4D3Eelectron microscopy2.12D125-332[»]
ProteinModelPortaliP18013.
SMRiP18013. Positions 39-322.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198214.CP0126.

Protein family/group databases

TCDBi1.C.36.3.1. the bacterial type iii-target cell pore (iiitcp) family.

Proteomic databases

PaxDbiP18013.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL72350; AAL72350; SF_p0126.
GeneIDi876444.
KEGGipg:20467558.
pg:876444.
sfl:CP0126.
PATRICi18722581. VBIShiFle86970_5381.

Phylogenomic databases

eggNOGiENOG4105IBT. Bacteria.
ENOG4111P3X. LUCA.
HOGENOMiHOG000012181.
KOiK13287.

Miscellaneous databases

EvolutionaryTraceiP18013.

Family and domain databases

InterProiIPR009483. Plasmid_invsIpaD.
IPR013386. T3SS_IpaD/SipD/SspD.
[Graphical view]
PfamiPF06511. IpaD. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02553. SipD_IpaD_SspD. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiIPAD_SHIFL
AccessioniPrimary (citable) accession number: P18013
Secondary accession number(s): Q6XVZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: September 7, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Deletion of amino acids 1-20 abolishes invasion activity, affects contact-mediated hemolysis activity and IpaD secretion. Deletion of amino acids 41-80 and 81-120 restores invasion activity to a higher level than wild-type and reduces contact-mediated hemolysis activity. Deletion beyond amino acid 120 reduces invasion activity and abolishes contact-mediated hemolysis activity.

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.