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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
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)DescriptionActionsGraphical viewLength
Topological domaini53 – 807ExtracellularSequence analysisAdd BLAST755
Transmembranei808 – 816Beta strandedSequence analysis9
Topological domaini817 – 818PeriplasmicSequence analysis2
Transmembranei819 – 827Beta strandedSequence analysis9
Topological domaini828 – 845ExtracellularSequence analysisAdd BLAST18
Transmembranei846 – 854Beta strandedSequence analysis9
Topological domaini855 – 862PeriplasmicSequence analysis8
Transmembranei863 – 871Beta strandedSequence analysis9
Topological domaini872 – 911ExtracellularSequence analysisAdd BLAST40
Transmembranei912 – 920Beta strandedSequence analysis9
Topological domaini921 – 924PeriplasmicSequence analysis4
Transmembranei925 – 933Beta strandedSequence analysis9
Topological domaini934 – 941ExtracellularSequence analysis8
Transmembranei942 – 950Beta strandedSequence analysis9
Topological domaini951 – 954PeriplasmicSequence analysis4
Transmembranei955 – 963Beta strandedSequence analysis9
Topological domaini964 – 968ExtracellularSequence analysis5
Transmembranei969 – 977Beta strandedSequence analysis9
Topological domaini978 – 981PeriplasmicSequence analysis4
Transmembranei982 – 990Beta strandedSequence analysis9
Topological domaini991 – 1002ExtracellularSequence analysisAdd BLAST12
Transmembranei1003 – 1011Beta strandedSequence analysis9
Topological domaini1012 – 1026PeriplasmicSequence analysisAdd BLAST15
Transmembranei1027 – 1035Beta strandedSequence analysis9
Topological domaini1036 – 1059ExtracellularSequence analysisAdd BLAST24
Transmembranei1060 – 1068Beta strandedSequence analysis9
Topological domaini1069 – 1071PeriplasmicSequence analysis3
Transmembranei1072 – 1080Beta strandedSequence analysis9
Topological domaini1081 – 1093ExtracellularSequence analysisAdd BLAST13
Transmembranei1094 – 1102Beta strandedSequence analysis9

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane, Periplasm, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi40G → E: Disrupts targeting to outer membrane. 1 Publication1
Mutagenesisi44L → R: Disrupts targeting to outer membrane. 1 Publication1
Mutagenesisi45L → R: Disrupts targeting to outer membrane. 1 Publication1
Mutagenesisi50A → R: Disrupts targeting to outer membrane. 1 Publication1
Mutagenesisi52A → R: Disrupts targeting to outer membrane. 1 Publication1
Mutagenesisi756 – 762SSRRASS → WQDDAPR: Loss of phosphorylation. 1 Publication7
Mutagenesisi758 – 759RR → DD: Abolishes cleavage by IcsP. Loss of phosphorylation. 1 Publication2
Mutagenesisi758R → D: Abolishes cleavage by IcsP. 1
Mutagenesisi759R → D: Loss of phosphorylation. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 521 PublicationAdd BLAST52
ChainiPRO_000038757453 – 1102Outer membrane protein IcsA autotransporterAdd BLAST1050
ChainiPRO_000000270053 – 758Outer membrane protein IcsAAdd BLAST706
ChainiPRO_0000002701759 – 1102Outer membrane protein IcsA translocatorAdd BLAST344

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)DescriptionActionsGraphical viewLength
Sitei758 – 759Cleavage; by IcsP2

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

11102
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi592 – 595Combined sources4
Beta strandi601 – 604Combined sources4
Beta strandi608 – 612Combined sources5
Beta strandi614 – 616Combined sources3
Beta strandi621 – 623Combined sources3
Helixi628 – 630Combined sources3
Beta strandi634 – 639Combined sources6
Beta strandi641 – 652Combined sources12
Beta strandi663 – 682Combined sources20
Beta strandi692 – 696Combined sources5
Beta strandi698 – 700Combined sources3
Beta strandi704 – 707Combined sources4
Beta strandi711 – 713Combined sources3
Beta strandi716 – 723Combined sources8
Beta strandi732 – 739Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ML3X-ray2.00A591-758[»]
ProteinModelPortaliQ7BCK4.
SMRiQ7BCK4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini814 – 1102AutotransporterPROSITE-ProRule annotationAdd BLAST289

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni53 – 758AlphaAdd BLAST706
Regioni320 – 433Interaction with APG5L and IcsBAdd BLAST114

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi117 – 332Gly-richAdd BLAST216

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)DescriptionActionsGraphical viewLength
Natural varianti53T → I in plasmid pINV_F6_M1382. 1
Natural varianti279V → I in plasmid pINV_F6_M1382. 1
Natural varianti667A → T in plasmid pINV_F6_M1382. 1
Natural varianti725V → A in plasmid pWR100. 1
Natural varianti923S → G in plasmid pINV_F6_M1382. 1
Natural varianti961A → T in plasmid pINV_F6_M1382. 1
Natural varianti1000G → V in plasmid pINV_F6_M1382. 1
Natural varianti1016Q → H in plasmid pINV_F6_M1382. 1

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.
WP_001071795.1. NZ_LVJC01000142.1.

Genome annotation databases

EnsemblBacteriaiAAL72293; AAL72293; SF_p0182.
GeneIDi1238021.
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.
WP_001071795.1. NZ_LVJC01000142.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ML3X-ray2.00A591-758[»]
ProteinModelPortaliQ7BCK4.
SMRiQ7BCK4.
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.
GeneIDi1238021.
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: November 2, 2016
This is version 91 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.