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