ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P18011


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name IPAB_SHIFL
Primary accession number P18011
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1990
Sequence was last modified on February 1, 1994 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 66)
Name and origin of the protein
Protein name Invasin ipaB
Synonym 62 kDa antigen
Gene name
Name: ipaB
OrderedLocusNames: CP0128
From
Shigella flexneri [TaxID: 623] [HAMAP proteome]
Encoded on Plasmid pWR100; Plasmid pMYSH6000; Plasmid pCP301.
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Shigella.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PLASMID=pWR100;
STRAIN=M90T / Serotype 5a;
DOI=10.1016/0882-4010(88)90062-9; PubMed=3071655 [NCBI, ExPASy, EBI, Israel, Japan]
Baudry B., Kaczorek M., Sansonetti P.J.;
"Nucleotide sequence of the invasion plasmid antigen B and C genes (ipaB and ipaC) of Shigella flexneri.";
Microb. Pathog. 4:345-357(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PLASMID=pWR100;
STRAIN=M90T / Serotype 5a;
PubMed=3057506 [NCBI, ExPASy, EBI, Israel, Japan]
Venkatesan M.M., Buysse J.M., Kopecko D.J.;
"Characterization of invasion plasmid antigen genes (ipaBCD) from Shigella flexneri.";
Proc. Natl. Acad. Sci. U.S.A. 85:9317-9321(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PLASMID=pWR100;
STRAIN=M90T / Serotype 5a;
PubMed=11115111 [NCBI, ExPASy, EBI, Israel, Japan]
Buchrieser C., Glaser P., Rusniok C., Nedjari H., d'Hauteville H., Kunst F., Sansonetti P.J., Parsot C.;
"The virulence plasmid pWR100 and the repertoire of proteins secreted by the type III secretion apparatus of Shigella flexneri.";
Mol. Microbiol. 38:760-771(2000).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PLASMID=pWR100;
STRAIN=M90T / Serotype 5a;
DOI=10.1128/IAI.69.5.3271-3285.2001; PubMed=11292750 [NCBI, ExPASy, EBI, Israel, Japan]
Venkatesan M.M., Goldberg M.B., Rose D.J., Grotbeck E.J., Burland V., Blattner F.R.;
"Complete DNA sequence and analysis of the large virulence plasmid of Shigella flexneri.";
Infect. Immun. 69:3271-3285(2001).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PLASMID=pMYSH6000;
STRAIN=YSH6000 / Serotype 2a;
PubMed=2552264 [NCBI, ExPASy, EBI, Israel, Japan]
Sasakawa C., Adler B., Tobe T., Okada N., Nagai S., Komatsu K., Yoshikawa M.;
"Functional organization and nucleotide sequence of virulence region-2 on the large virulence plasmid in Shigella flexneri 2a.";
Mol. Microbiol. 3:1191-1201(1989).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PLASMID=pCP301;
STRAIN=301 / Serotype 2a;
DOI=10.1093/nar/gkf566; PubMed=12384590 [NCBI, ExPASy, EBI, Israel, Japan]
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157.";
Nucleic Acids Res. 30:4432-4441(2002).
[7]
FUNCTION IN APOPTOSIS.
PubMed=9009343 [NCBI, ExPASy, EBI, Israel, Japan]
Thirumalai K., Kim K.-S., Zychlinsky A.;
"IpaB, a Shigella flexneri invasin, colocalizes with interleukin-1 beta-converting enzyme in the cytoplasm of macrophages.";
Infect. Immun. 65:787-793(1997).
[8]
REVIEW.
DOI=10.1046/j.1462-5822.2000.00046.x; PubMed=11207575 [NCBI, ExPASy, EBI, Israel, Japan]
Tran Van Nhieu G., Bourdet-Sicard R., Dumenil G., Blocker A., Sansonetti P.J.;
"Bacterial signals and cell responses during Shigella entry into epithelial cells.";
Cell. Microbiol. 2:187-193(2000).
Comments
  • FUNCTION: Forms a pore with ipaC, which is inserted into the host cell membrane through the Mxi/Spa apparatus, during cell contact. This pore probably allows the translocation of ipaA. IpaB has also been found to be necessary and sufficient to activate macrophage apoptosis by binding to interleukin-1 beta converting enzyme (ICE). Has also been shown to be important, along with ipaD, to block or regulate secretion through the Mxi/Spa translocon in the presence or absence of the secretion signal, respectively.
  • INTERACTION:
    P29452:Casp1 (xeno); NbExp=3; IntAct=EBI-490239, EBI-489700;
    P16070:CD44 (xeno); NbExp=4; IntAct=EBI-490239, EBI-490245;
    Q9UI95:MAD2L2 (xeno); NbExp=4; IntAct=EBI-490239, EBI-77889;
  • SUBCELLULAR LOCATION: Secreted. Note=Secreted through the specialized type-III secretion system Mxi/Spa. Inserted into the host cell membrane. Also secreted into the host cell cytoplasm after the escape of bacteria from phagosome, where it colocalizes with ICE.
  • INDUCTION: Synthesis of this immunogen is repressed at 30 degrees Celsius and restored at 37 degrees Celsius.
  • SIMILARITY: Belongs to the invasin protein B family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J04117; AAA26522.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M34849; AAA98424.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391753; CAC05803.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF348706; AAK18446.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X15319; CAA33381.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF386526; AAL72352.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A34965; A34965.
RefSeq NP_085290.1; -.
NP_858261.1; -.
3D structure databases
ModBase P18011.
Protein-protein interaction databases
IntAct P18011; -.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR003895; Invas_B.
Graphical view of domain structure.
Pfam PF03518; Invas_B; 1.
Pfam graphical view of domain structure.
PRINTS PR01375; BACINVASINB.
BLOCKS P18011.
Genome annotation databases
GeneID 1238055; -.
876451; -.
GenomeReviews AF386526_GR; CP0128.
KEGG sfl:CP0128; -.
Phylogenomic databases
HOGENOM P18011; -.
Genome annotation databases
CMR P18011; CP0128.
Other
ProtoNet P18011.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Membrane; Plasmid; Secreted; Transmembrane; Virulence.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   580  580     Invasin ipaB. PRO_0000219853
TRANSMEM   313   333  21     Potential. 
TRANSMEM   399   419  21     Potential. 
VARIANT   18    18  1     T -> A (in plasmid pMYSH6000 and plasmid pCP301). 
CONFLICT   167   167        E -> N (in Ref. 2; AAA26522). 
Sequence information
Length: 580 AA [This is the length of the unprocessed precursor] Molecular weight: 62201 Da [This is the MW of the unprocessed precursor] CRC64: 56325105E4BC0F70 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MHNVSTTTTG FPLAKILTST ELGDNTIQAA NDAANKLFSL TIADLTANQN INTTNAHSTS 

        70         80         90        100        110        120 
NILIPELKAP KSLNASSQLT LLIGNLIQIL GEKSLTALTN KITAWKSQQQ ARQQKNLEFS 

       130        140        150        160        170        180 
DKINTLLSET EGLTRDYEKQ INKLKNADSK IKDLENKINQ IQTRLSELDP ESPEKKKLSR 

       190        200        210        220        230        240 
EEIQLTIKKD AAVKDRTLIE QKTLSIHSKL TDKSMQLEKE IDSFSAFSNT ASAEQLSTQQ 

       250        260        270        280        290        300 
KSLTGLASVT QLMATFIQLV GKNNEESLKN DLALFQSLQE SRKTEMERKS DEYAAEVRKA 

       310        320        330        340        350        360 
EELNRVMGCV GKILGALLTI VSVVAAAFSG GASLALAAVG LALMVTDAIV QAATGNSFME 

       370        380        390        400        410        420 
QALNPIMKAV IEPLIKLLSD AFTKMLEGLG VDSKKAKMIG SILGAIAGAL VLVAAVVLVA 

       430        440        450        460        470        480 
TVGKQAAAKL AENIGKIIGK TLTDLIPKFL KNFSSQLDDL ITNAVARLNK FLGAAGDEVI 

       490        500        510        520        530        540 
SKQIISTHLN QAVLLGESVN SATQAGGSVA SAVFQNSAST NLADLTLSKY QVEQLSKYIS 

       550        560        570        580 
EAIEKFGQLQ EVIADLLASM SNSQANRTDV AKAILQQTTA 

P18011 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!