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1.C.36.3.1
IIITCP protein complex, IpaB/IpaC/IpaD. Physical contact with host cells initiates secretion and leads to assembly of a pore, IpaB/IpaC, in the host cell membrane. The active needle tip complex of S. flexneri is composed of a tip protein, IpaD, and the two pore-forming proteins, IpaB and IpaC. The atomic structures of IpaD and a protease-stable coiled-coil fragment in the N-terminal regions of IpaB from S. flexneri and the homologous SipB from Salmonella enterica have been determined (Barta et al. 2012).  Structural comparisons revealed similarity to the coiled-coil regions of pore-forming proteins such as colicin Ia (TC# 1.C.1.1.1).  Interaction between IpaB and IpaD at the needle tip is key to host cell sensing, orchestration of IpaC secretion and its subsequent assembly at needle tips (Veenendaal et al. 2007). The N-terminus of IpaC is extracellular and the C-terminus is intracellular, and its topology has been studied (Russo et al. 2019). Residures lining the pore channel of the plasma membrane-embedded Shigella flexneri type 3 secretion translocase, IpaB, have been identified (Chen et al. 2021).

Accession Number:Q03945
Protein Name:IpaB
Length:580
Molecular Weight:62170.00
Species:Shigella dysenteriae [622]
Number of TMSs:4
Location1 / Topology2 / Orientation3: Secreted1 / Multi-pass membrane protein2
Substrate

Cross database links:

Gene Ontology

GO:0020002 C:host cell plasma membrane
GO:0016021 C:integral to membrane
GO:0009405 P:pathogenesis

References (1)

[1] “Nucleotide sequence of the ipaBCD structural genes of Shigella dysenteriae.”  Yao R.et.al.   1766387

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MHNVNTTTTG LSLAKILAST ELGDNTIQAG NDAANKLFSL TIADLTANKN INTTNAHSTS 
61:	NILIPELKAP KSLNASSQLT LLIGNLIQIL GEKSLTALTN KITAWKSQQQ ARQQKNLEFS 
121:	DKINTLLSET EGLTRDYEKQ INKLKNADSK IKDLENKINQ IQTRLSELDP DSPEKKKLSR 
181:	EEIQLTIKKD AAVKDRTLIE QKTLSIHSKL TDKSMQLEKE IDSFSAFSNT ASAEQLSTQQ 
241:	KSLTGLASVT QLMATFIQLV GKNNEESLKN DLALFQSLQE SRKTEMERKS DEYAAEVRKA 
301:	EELNRVMGCV GKILGALLTI VSVVAAAFSG GASLALADVG LALMVTDAIV QAATGNSFME 
361:	QALNPIMKAV IEPLIKLLSD AFTKMLEGLG VDSKKAKMIG SILGAIAGAL VLVAAVVLVA 
421:	TVGKQAAAKL AENIGKIIGK TLTDLIPKFL KNFSSQLDDL ITNAVARLNK FLGAAGDEVI 
481:	SKQIISTHLN QAVLLGESVN SATQAGGSVA SAVFQNSAST NLADLTLSKY QVEQLSKYIS 
541:	EAIEKFGQLQ EVIADLLASM SNSQANRTDV AKAILQQTTA