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Protein

Outer membrane protein IcsA autotransporter

Gene

icsA

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

Functioni

Essential for bacterial spreading by eliciting polar deposition of filamentous actin (actin-based motility). Inside the host cell mediates nucleation and polymerization of actin molecules on the bacterial surface, which provides the propulsive force for intracellular movement and intercellular dissemination of the bacterium. During invasion of mammalian cells, triggers autophagy by binding to APG5L. Interaction with IcsB leads to escape from the autophagic host defense system. Also binds ATP and displays weak ATPase activity.5 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Virulence

Protein family/group databases

TCDBi1.B.12.1.2. the autotransporter-1 (at-1) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Outer membrane protein IcsA autotransporter
Cleaved into the following 2 chains:
Gene namesi
Name:icsA
Synonyms:virG
Ordered Locus Names:CP0182
Encoded oniPlasmid pWR1009 Publications
Plasmid pMYSH60006 Publications
Plasmid pINV_F6_M13821 Publication
Plasmid pCP3011 Publication
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
Proteomesi
  • UP000001006 Componenti: Plasmid pCP301

Subcellular locationi

Outer membrane protein IcsA :
  • Secreted
  • Cell surface

  • Note: The alpha domain is localized as a cap over the old pole of the bacterial surface.
Outer membrane protein IcsA translocator :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini53 – 807755ExtracellularSequence analysisAdd
BLAST
Transmembranei808 – 8169Beta strandedSequence analysis
Topological domaini817 – 8182PeriplasmicSequence analysis
Transmembranei819 – 8279Beta strandedSequence analysis
Topological domaini828 – 84518ExtracellularSequence analysisAdd
BLAST
Transmembranei846 – 8549Beta strandedSequence analysis
Topological domaini855 – 8628PeriplasmicSequence analysis
Transmembranei863 – 8719Beta strandedSequence analysis
Topological domaini872 – 91140ExtracellularSequence analysisAdd
BLAST
Transmembranei912 – 9209Beta strandedSequence analysis
Topological domaini921 – 9244PeriplasmicSequence analysis
Transmembranei925 – 9339Beta strandedSequence analysis
Topological domaini934 – 9418ExtracellularSequence analysis
Transmembranei942 – 9509Beta strandedSequence analysis
Topological domaini951 – 9544PeriplasmicSequence analysis
Transmembranei955 – 9639Beta strandedSequence analysis
Topological domaini964 – 9685ExtracellularSequence analysis
Transmembranei969 – 9779Beta strandedSequence analysis
Topological domaini978 – 9814PeriplasmicSequence analysis
Transmembranei982 – 9909Beta strandedSequence analysis
Topological domaini991 – 100212ExtracellularSequence analysisAdd
BLAST
Transmembranei1003 – 10119Beta strandedSequence analysis
Topological domaini1012 – 102615PeriplasmicSequence analysisAdd
BLAST
Transmembranei1027 – 10359Beta strandedSequence analysis
Topological domaini1036 – 105924ExtracellularSequence analysisAdd
BLAST
Transmembranei1060 – 10689Beta strandedSequence analysis
Topological domaini1069 – 10713PeriplasmicSequence analysis
Transmembranei1072 – 10809Beta strandedSequence analysis
Topological domaini1081 – 109313ExtracellularSequence analysisAdd
BLAST
Transmembranei1094 – 11029Beta strandedSequence analysis

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane, Periplasm, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 401G → E: Disrupts targeting to outer membrane. 1 Publication
Mutagenesisi44 – 441L → R: Disrupts targeting to outer membrane. 1 Publication
Mutagenesisi45 – 451L → R: Disrupts targeting to outer membrane. 1 Publication
Mutagenesisi50 – 501A → R: Disrupts targeting to outer membrane. 1 Publication
Mutagenesisi52 – 521A → R: Disrupts targeting to outer membrane. 1 Publication
Mutagenesisi756 – 7627SSRRASS → WQDDAPR: Loss of phosphorylation. 1 Publication
Mutagenesisi758 – 7592RR → DD: Abolishes cleavage by IcsP. Loss of phosphorylation. 1 Publication
Mutagenesisi758 – 7581R → D: Abolishes cleavage by IcsP.
Mutagenesisi759 – 7591R → D: Loss of phosphorylation.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 52521 PublicationAdd
BLAST
Chaini53 – 11021050Outer membrane protein IcsA autotransporterPRO_0000387574Add
BLAST
Chaini53 – 758706Outer membrane protein IcsAPRO_0000002700Add
BLAST
Chaini759 – 1102344Outer membrane protein IcsA translocatorPRO_0000002701Add
BLAST

Post-translational modificationi

Phosphorylated by host cAMP-dependent protein kinase, which may represent a host defense mechanism during the invasion process.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei758 – 7592Cleavage; by IcsP

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ7BCK4.
PRIDEiQ7BCK4.

Miscellaneous databases

PMAP-CutDBQ7BCK4.

Expressioni

Inductioni

Transcriptionally regulated by VirF.

Interactioni

Subunit structurei

Forms a ternary complex with host WASL (neural Wiskott-Aldrich syndrome protein) and ARP2/3. IcsA enhances the affinity of WASL for ARP2/3, thus assembling a tight complex which has maximal activity in actin assembly. Also binds directly to host vinculin, which may serve as an actin filament recruiter.

Protein-protein interaction databases

MINTiMINT-1535081.
STRINGi198214.CP0182.

Structurei

Secondary structure

1
1102
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi592 – 5954Combined sources
Beta strandi601 – 6044Combined sources
Beta strandi608 – 6125Combined sources
Beta strandi614 – 6163Combined sources
Beta strandi621 – 6233Combined sources
Helixi628 – 6303Combined sources
Beta strandi634 – 6396Combined sources
Beta strandi641 – 65212Combined sources
Beta strandi663 – 68220Combined sources
Beta strandi692 – 6965Combined sources
Beta strandi698 – 7003Combined sources
Beta strandi704 – 7074Combined sources
Beta strandi711 – 7133Combined sources
Beta strandi716 – 7238Combined sources
Beta strandi732 – 7398Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ML3X-ray2.00A591-758[»]
ProteinModelPortaliQ7BCK4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini814 – 1102289AutotransporterPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 758706AlphaAdd
BLAST
Regioni320 – 433114Interaction with APG5L and IcsBAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi117 – 332216Gly-richAdd
BLAST

Domaini

The signal peptide, cleaved at the inner membrane, guides the autotransporter protein to the periplasmic space. Then, insertion of the C-terminal translocator domain (or beta domain) in the outer membrane forms a hydrophilic pore for the translocation of the passenger domain (or alpha domain) to the bacterial cell surface, where IcsA is cleaved by IcsP (SopA) and released into the extracellular medium. This cleavage is important for the maintenance of the sharply polarized distribution of IcsA but is not a prerequisite for intracellular spreading.
The glycine-rich domain interacts with the WASL CRIB domain.

Sequence similaritiesi

Contains 1 autotransporter (TC 1.B.12) domain. [View classification]PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiENOG4106AS2. Bacteria.
COG3468. LUCA.
HOGENOMiHOG000034746.
KOiK12679.
OMAiDAWLQYG.

Family and domain databases

Gene3Di2.160.20.20. 1 hit.
2.40.128.130. 1 hit.
InterProiIPR005546. Autotransporte_beta.
IPR013425. Autotrns_rpt.
IPR006315. OM_autotransptr_brl.
IPR012332. P22_tailspike_C-like.
IPR011050. Pectin_lyase_fold/virulence.
IPR004899. Pertactin_central.
[Graphical view]
PfamiPF03797. Autotransporter. 1 hit.
PF12951. PATR. 1 hit.
PF03212. Pertactin. 1 hit.
[Graphical view]
SMARTiSM00869. Autotransporter. 1 hit.
[Graphical view]
SUPFAMiSSF103515. SSF103515. 1 hit.
SSF51126. SSF51126. 2 hits.
TIGRFAMsiTIGR01414. autotrans_barl. 1 hit.
TIGR02601. autotrns_rpt. 1 hit.
PROSITEiPS51208. AUTOTRANSPORTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q7BCK4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNQIHKFFCN MTQCSQGGAG ELPTVKEKTC KLSFSPFVVG ASLLLGGPIA
60 70 80 90 100
FATPLSGTQE LHFSEDNYEK LLTPVDGLSP LGAGEDGMDA WYITSSNPSH
110 120 130 140 150
ASRTKLRINS DIMISAGHGG AGDNNDGNSC GGNGGDSITG SDLSIINQGM
160 170 180 190 200
ILGGSGGSGA DHNGDGGEAV TGDNLFIING EIISGGHGGD SYSDSDGGNG
210 220 230 240 250
GDAVTGVNLP IINKGTISGG NGGNNYGEGD GGNGGDAITG SSLSVINKGT
260 270 280 290 300
FAGGNGGAAY GYGYDGYGGN AITGDNLSVI NNGAILGGNG GHWGDAINGS
310 320 330 340 350
NMTIANSGYI ISGKEDDGTQ NVAGNAIHIT GGNNSLILHE GSVITGDVQV
360 370 380 390 400
NNSSILKIIN NDYTGTTPTI EGDLCAGDCT TVSLSGNKFT VSGDVSFGEN
410 420 430 440 450
SSLNLAGISS LEASGNMSFG NNVKVEAIIN NWAQKDYKLL SADKGITGFS
460 470 480 490 500
VSNISIINPL LTTGAIDYTK SYISDQNKLI YGLSWNDTDG DSHGEFNLKE
510 520 530 540 550
NAELTVSTIL ADNLSHHNIN SWDGKSLTKS GEGTLILAEK NTYSGFTNIN
560 570 580 590 600
AGILKMGTVE AMTRTAGVIV NKGATLNFSG MNQTVNTLLN SGTVLINNIN
610 620 630 640 650
APFLPDPVIV TGNMTLEKNG HVILNNSSSN VGQTYVQKGN WHGKGGILSL
660 670 680 690 700
GAVLGNDNSK TDRLEIAGHA SGITYVAVTN EGGSGDKTLE GVQIISTDSS
710 720 730 740 750
DKNAFIQKGR IVAGSYDYRL KQGTVSGLNT NKWYLTSQMD NQESKQMSNQ
760 770 780 790 800
ESTQMSSRRA SSQLVSSLNL GEGSIHTWRP EAGSYIANLI AMNTMFSPSL
810 820 830 840 850
YDRHGSTIVD PTTGQLSETT MWIRTVGGHN EHNLADRQLK TTANRMVYQI
860 870 880 890 900
GGDILKTNFT DHDGLHVGIM GAYGYQDSKT HNKYTSYSSR GTVSGYTAGL
910 920 930 940 950
YSSWFQDEKE RTGLYMDAWL QYSWFNNTVK GDGLTGEKYS SKGITGALEA
960 970 980 990 1000
GYIYPTIRWT AHNNIDNALY LNPQVQITRH GVKANDYIEH NGTMVTSSGG
1010 1020 1030 1040 1050
NNIQAKLGLR TSLISQSCID KETLRKFEPF LEVNWKWSSK QYGVIMNGMS
1060 1070 1080 1090 1100
NHQIGNRNVI ELKTGVGGRL ADNLSIWGNV SQQLGNNSYR DTQGILGVKY

TF
Length:1,102
Mass (Da):116,244
Last modified:July 5, 2004 - v1
Checksum:i5F6A1E353B105B9F
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti53 – 531T → I in plasmid pINV_F6_M1382.
Natural varianti279 – 2791V → I in plasmid pINV_F6_M1382.
Natural varianti667 – 6671A → T in plasmid pINV_F6_M1382.
Natural varianti725 – 7251V → A in plasmid pWR100.
Natural varianti923 – 9231S → G in plasmid pINV_F6_M1382.
Natural varianti961 – 9611A → T in plasmid pINV_F6_M1382.
Natural varianti1000 – 10001G → V in plasmid pINV_F6_M1382.
Natural varianti1016 – 10161Q → H in plasmid pINV_F6_M1382.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22802 Genomic DNA. Translation: AAA26547.1.
AL391753 Genomic DNA. Translation: CAC05837.1.
AF348706 Genomic DNA. Translation: AAK18502.1.
AY294290 Genomic DNA. Translation: AAQ57625.1.
AF386526 Genomic DNA. Translation: AAL72293.1.
PIRiA32247.
RefSeqiNP_858315.1. NC_004851.1.

Genome annotation databases

EnsemblBacteriaiAAL72293; AAL72293; SF_p0182.
KEGGisfl:CP0182.
PATRICi18722683. VBIShiFle86970_5433.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22802 Genomic DNA. Translation: AAA26547.1.
AL391753 Genomic DNA. Translation: CAC05837.1.
AF348706 Genomic DNA. Translation: AAK18502.1.
AY294290 Genomic DNA. Translation: AAQ57625.1.
AF386526 Genomic DNA. Translation: AAL72293.1.
PIRiA32247.
RefSeqiNP_858315.1. NC_004851.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ML3X-ray2.00A591-758[»]
ProteinModelPortaliQ7BCK4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1535081.
STRINGi198214.CP0182.

Protein family/group databases

TCDBi1.B.12.1.2. the autotransporter-1 (at-1) family.

Proteomic databases

PaxDbiQ7BCK4.
PRIDEiQ7BCK4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL72293; AAL72293; SF_p0182.
KEGGisfl:CP0182.
PATRICi18722683. VBIShiFle86970_5433.

Phylogenomic databases

eggNOGiENOG4106AS2. Bacteria.
COG3468. LUCA.
HOGENOMiHOG000034746.
KOiK12679.
OMAiDAWLQYG.

Miscellaneous databases

PMAP-CutDBQ7BCK4.

Family and domain databases

Gene3Di2.160.20.20. 1 hit.
2.40.128.130. 1 hit.
InterProiIPR005546. Autotransporte_beta.
IPR013425. Autotrns_rpt.
IPR006315. OM_autotransptr_brl.
IPR012332. P22_tailspike_C-like.
IPR011050. Pectin_lyase_fold/virulence.
IPR004899. Pertactin_central.
[Graphical view]
PfamiPF03797. Autotransporter. 1 hit.
PF12951. PATR. 1 hit.
PF03212. Pertactin. 1 hit.
[Graphical view]
SMARTiSM00869. Autotransporter. 1 hit.
[Graphical view]
SUPFAMiSSF103515. SSF103515. 1 hit.
SSF51126. SSF51126. 2 hits.
TIGRFAMsiTIGR01414. autotrans_barl. 1 hit.
TIGR02601. autotrns_rpt. 1 hit.
PROSITEiPS51208. AUTOTRANSPORTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiICSA_SHIFL
AccessioniPrimary (citable) accession number: Q7BCK4
Secondary accession number(s): Q52298, Q6WE27, Q99Q93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: July 5, 2004
Last modified: September 7, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Secretion across inner membrane is dependent on the SecA and SecYEG apparatus. However, the polar localization comes before secretion and is independent of SecA.
Deletion experiments show that amino acids 58-103, 505-537 and 507-729 are required for polar localization and that amino acids 102-779 are responsible for interaction with APG5L and IcsB.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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.