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SabA family sialic acid-binding adhesin
This is the N-terminal extracellular adhesion domain of Sialic acid binding adhesin (SabA) present in Helicobacter pylori. The N-terminal domain of SabA functions as a sugar-binding adhesion domain with conserved disulfide bonds. Notably, these amino acid residues are not only conserved among SabA orthologs but also between SabA and BabA [1]. [1]. 24375407. The three-dimensional structure of the extracellular adhesion domain of the sialic acid-binding adhesin SabA from Helicobacter pylori. Pang SS, Nguyen ST, Perry AJ, Day CJ, Panjikar S, Tiralongo J, Whisstock JC, Kwok T;. J Biol Chem. 2014;289:6332-6340. (from Pfam)
outer membrane beta-barrel protein
This family seems confined to Helicobacter. It is predicted to be an outer membrane protein based on its pattern of alternating hydrophobic amino acids similar to porins [1]. See alignment Figure 3 and caption. [1]. 9252185. The complete genome sequence of the gastric pathogen Helicobacter pylori [see comments] [published erratum appears in Nature 1997 Sep 25;389(6649):412]. Tomb JF, White O, Kerlavage AR, Clayton RA, Sutton GG, Fleischmann RD, Ketchum KA, Klenk HP, Gill S, Dougherty BA, Nelson K, Quackenbush J, Zhou L, Kirkness EF, Peterson S, Loftus B, Richardson D, Dodson R, Khalak HG, Glodek A, McKenney K, Fitzegerald LM,. Nature 1997;388:539-547. (from Pfam)
outer membrane protein
outer membrane protein similar to Helicobacter pylori Hop family proteins and BabA adhesin, which mediates binding to fucosylated ABH antigens of the ABO blood group
Hop family adhesin SabA
SabA (sialic acid binding adhesin), as found in Helicobacter pylori, is an outer membrane beta-barrel domain-containing protein that contributes to binding to the gastric mucosa. It belongs to the Hop family, along with paralogs SabB, BabA, BabB, and HopZ, which likewise serve as adhesins. Changes in the length of nucleotide repeats cause phase variation, blocking expression of SabA in many strains.
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