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1.B.1.1.15
OmpU porin (cation-selective; PK/PCl = 14; bile salt inducible) (low permeability to bile) (Simonet et al., 2003). OmpU influences sensitivities to β-lactam antibiotics and sodium deoxycholate induction of biofilm formation and growth on large sugars (Pagel et al., 2007).   The effective pore radus is 0.55 nm which increases with acidic pH but decreases with increasing ionic strength (Duret and Delcour 2010). OmpU induces target animal cell death after it inserts into host mitochondrial membranes (Gupta et al. 2015). The high resolution structures of OmpT and OmpU, the two major porins in V. cholerae, have been determined, and both have unusual constrictions that create narrower barriers for small-molecule permeation and change the internal electric fields of the channels (Pathania et al. 2018). Vibrio cholerae OmpU activates dendritic cells via TLR2 and the NLRP3 inflammasome (Dhar et al. 2023).

Accession Number:P0C6Q6
Protein Name:Outer membrane protein U
Length:341
Molecular Weight:36645.00
Species:Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [243277]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Cell outer membrane1 / Multi-pass membrane protein2
Substrate cation, beta-lactam antibiotic, sodium dodecyl sulfate

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Structure:
5ONU     

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FASTA formatted sequence
1:	MNKTLIALAV SAAAVATGAY ADGINQSGDK AGSTVYSAKG TSLEVGGRAE ARLSLKDGKA 
61:	QDNSRVRLNF LGKAEINDSL YGVGFYEGEF TTNDQGKNAS NNSLDNRYTY AGIGGTYGEV 
121:	TYGKNDGALG VITDFTDIMS YHGNTAAEKI AVADRVDNML AYKGQFGDLG VKASYRFADR 
181:	NAVDAMGNVV TETNAAKYSD NGEDGYSLSA IYTFGDTGFN VGAGYADQDD QNEYMLAASY 
241:	RMENLYFAGL FTDGELAKDV DYTGYELAAG YKLGQAAFTA TYNNAETAKE TSADNFAIDA 
301:	TYYFKPNFRS YISYQFNLLD SDKVGKVASE DELAIGLRYD F