TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*1.B.21.1.1









Non-specific, 14 β-stranded monomeric OmpG porin (Conlan et al. 2000). pH-induced conformational changes of OmpG have been studied after reconstitution in native E. coli lipids (Mari et al., 2010).  Encoded by a gene in a gene cluster also encoding an ABC sugar uptake system (TC# 3.A.1.1.46), a glucosyl hydrolase and two oxidoreductases.  Therefore it's phsiological function may be glucoside uptake. At neutral/high pH, the channel is open and permeable to substrates of size up to 900Da. At acidic pH, loop L6 folds across the channel and blocks the pore. The channel blockage at acidic pH appears to be triggered by the protonation of a histidine pair on neighboring β-strands, which repel one another, resulting in the rearrangement of loop L6 and channel closure (Köster et al. 2015).  Crystallization and analysis by electron microscopy and X-ray crystallography revealed the fundamental mechanisms essential for the channel activity.  A 28 aa extension has been added to the 14 β-TMS barrel to make a 16 β-TMS barrel with normal activity and stability but differing pH sensitivity (Korkmaz et al. 2015).

Bacteria
Proteobacteria
OmpG of E. coli
*1.B.21.1.2









Putative porin

Bacteria
Fusobacteria
Putative porin of Fusobacterium mortiferum
*1.B.21.1.3









Uncharacterized protein of 355 aas

Bacteria
Fusobacteria
UP of Sebaldella termitidis
*1.B.21.2.1









Putative porin

Bacteria
Proteobacteria
Putative porin of E. coli
*1.B.21.2.2









Putative porin of 361 aas

Bacteria
Proteobacteria
Putative porin of Providencia burhodogranariea
*1.B.21.3.1









Putative porin

Bacteria
Proteobacteria
Putative porin of Vibrio sinaloensis
*1.B.21.3.2









Putative porin

Bacteria
Proteobacteria
Putative porin of Vibrio harveyi
*1.B.21.3.3









Putative porin

Bacteria
Proteobacteria
Putative porin of Vibrio parahaemolyticus