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BapA/Bap/LapF family prefix-like domain-containing protein
This entry represents the N-terminal domain of two largely unrelated repetitive proteins, both named Biofilm-associated protein BapA (from Salmonella enterica and from Paracoccus denitrificans), which share common domains at the two ends. The conserved prefix (N-terminal) domain is shared by a number of other large, repetitive proteins from proteobacteria and are thought to be associated with adhesion or biofilm formation [1,2]. [1]. 16313619. BapA, a large secreted protein required for biofilm formation and host colonization of Salmonella enterica serovar Enteritidis. Latasa C, Roux A, Toledo-Arana A, Ghigo JM, Gamazo C, Penades JR, Lasa I;. Mol Microbiol. 2005;58:1322-1339. [2]. 28158695. Biofilm formation by Paracoccus denitrificans requires a type I secretion system-dependent adhesin BapA. Yoshida K, Toyofuku M, Obana N, Nomura N;. FEMS Microbiol Lett. 2017; [Epub ahead of print] (from Pfam)
Ig-like domain-containing protein
Presumed domain found as tandem repeats of high sequence identity in bacterial cell surface proteins. (from Pfam)
Ig-like domain repeat protein
This family consists of bacterial domains with an Ig-like fold. Members of this family are found in a variety of bacterial surface proteins. (from Pfam)
BapA prefix-like domain-containing protein
Two largely unrelated repetitive proteins, both named biofilm-associated protein BapA (from Salmonella enterica and from Paracoccus denitrificans) share homology domains at the two ends. Both lack a typical signal peptide for translocation by Sec, and instead depend on type I secretion for export and for contribution to biofilm formation. The conserved prefix (i.e. N-terminal) domain is shared by a number of other large, repetitive proteins of Proteobacteria thought to be associated with adhesion or biofilm formation.
Ca2+-stabilized repeat-containing adhesin
This repeat is found in proteins such as the biofilm-associated protein Bap of Acinetobacter baumannii (which can exceed 8000 amino acids in length), the calcium-stabilized ice-binding adhesin of the Antarctic bacterium Marinomonas primoryensis, and the giant calcium-binding adhesin SiiE of Salmonella enterica.
This variant form of the Ig-like domain occurs as a repeat in a number of large adhesins, including a 1.5-MDa ice-binding adhesin, the Marinomonas primoryensis antifreeze protein.
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