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1.B.1.8.1
Low ion selective porin (PK/PCl = 4), OmpT (high permeability to bile) (Simonet et al., 2003). OmpT has an effective radius of 0.43nm, and acidic pH, high ionic strength, or exposure to polyethyleneglycol stabilizes a less conductive state (Duret & Delcour, 2010).  It binds the biofilm matrix protein, Bap1, which influences antimicrobial peptide (polymyxin B and LL-37) resistance (Duperthuy et al. 2013). 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).

Accession Number:O86021
Protein Name:OmpT
Length:344
Molecular Weight:37168.00
Species:Vibrio cholerae [666]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Secreted1
Substrate ion

Cross database links:

Gene Ontology

GO:0016020 C:membrane
GO:0005215 F:transporter activity
GO:0006810 P:transport

References (1)

[1] “Molecular cloning and transcriptional regulation of ompT, a ToxR-repressed gene in Vibrio cholerae.”  Li C.C.et.al.   10632889
Structure:
5OYK     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MKKTLLALAV LAAAGSVNAA EILKSDAGTV DFYGQLRTEL KFLEDKDPTI GSGSSRAGVD 
61:	ANYTVNDSLA LQGKVEFALK DSGDMYVRNH ILGVKTNFGK FSFGKQWTTS DDVYGADYSY 
121:	FFGGTGLRYG TLSDALHDSQ VKYVYEADSF WVKAGYGFPE DNAKQELAEL YVGATFGDLA 
181:	VHAGGGQNRD KAFKVGSNTV GTTTTDIKAD VTNSYFEVTG EYTIGDALIG VTYYNAELDV 
241:	ENNPLVIDED AISVAGTYKV ADKTKLYAGY EYVMQEANTG ADEDGTLVYL GVEYKFASWA 
301:	RVYAEYGYGD GTTLGYTNKG SDAEVKATKV DSANNFGIGA RIYW