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Protein

Invasin IpaD

Gene

ipaD

Organism
Shigella flexneri
Status
Reviewed-Annotation score: -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

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.

GO - Biological processi

Keywordsi

Biological processVirulence

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
Proteomesi
  • UP000001006 Componenti: Plasmid pCP301

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi151K → E: 50% reduction in hemolytic activity; when associated with K-154. 1 Publication1
Mutagenesisi154E → K: 50% reduction in hemolytic activity; when associated with E-151. 1 Publication1
Mutagenesisi321 – 322SC → AS: Restores invasion activity in a nonpolar ipaD mutant. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002198621 – 332Invasin IpaDAdd BLAST332

Proteomic databases

PRIDEiP18013

Expressioni

Inductioni

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

Structurei

Secondary structure

1332
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi43 – 65Combined sources23
Beta strandi67 – 69Combined sources3
Helixi72 – 95Combined sources24
Helixi111 – 114Combined sources4
Helixi119 – 121Combined sources3
Beta strandi128 – 130Combined sources3
Helixi131 – 148Combined sources18
Helixi150 – 174Combined sources25
Helixi175 – 177Combined sources3
Beta strandi178 – 190Combined sources13
Helixi192 – 206Combined sources15
Beta strandi210 – 213Combined sources4
Beta strandi214 – 216Combined sources3
Helixi220 – 230Combined sources11
Turni232 – 234Combined sources3
Beta strandi235 – 239Combined sources5
Beta strandi241 – 248Combined sources8
Helixi251 – 262Combined sources12
Beta strandi265 – 267Combined sources3
Beta strandi269 – 271Combined sources3
Helixi273 – 317Combined sources45

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5VXJX-ray2.50A/C/E/G/I38-322[»]
5VXKX-ray2.55A39-322[»]
5VXLX-ray2.80A39-322[»]
5VXMX-ray2.05A39-322[»]
ProteinModelPortaliP18013
SMRiP18013
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18013

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni192 – 267IpaB bindingCuratedAdd BLAST76

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili44 – 77Sequence analysisAdd BLAST34

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

Gene3Di1.20.1710.10, 1 hit
InterProiView protein in InterPro
IPR036708 BipD-like_sf
IPR009483 Plasmid_invsIpaD
PfamiView protein in Pfam
PF06511 IpaD, 1 hit
SUPFAMiSSF140693 SSF140693, 1 hit
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)DescriptionActionsGraphical viewLength
Natural varianti64E → D in plasmid pINV_F6_M1382. 1
Natural varianti101 – 102RN → KK in plasmid pINV_F6_M1382. 2
Natural varianti102N → H in plasmid pMYSH6000 and plasmid pCP301. 1
Natural varianti126 – 127DQ → YE in plasmid pINV_F6_M1382. 2
Natural varianti136A → D in plasmid pINV_F6_M1382. 1
Natural varianti140N → K in plasmid pINV_F6_M1382. 1
Natural varianti144D → N in plasmid pINV_F6_M1382. 1
Natural varianti193N → K in plasmid pINV_F6_M1382. 1
Natural varianti197 – 201KALEE → DELTK in plasmid pINV_F6_M1382. 5
Natural varianti220Q → K in plasmid pINV_F6_M1382. 1
Natural varianti239Q → E in plasmid pINV_F6_M1382. 1
Natural varianti247S → N in plasmid pINV_F6_M1382. 1

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
GeneIDi1238053
876444
KEGGisfl:CP0126
PATRICifig|198214.7.peg.5381

Similar proteinsi

Entry informationi

Entry nameiIPAD_SHIFL
AccessioniPrimary (citable) accession number: P18013
Secondary accession number(s): Q6XVZ1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: April 25, 2018
This is version 123 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
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Main funding by: National Institutes of Health