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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)
This domain is found in a wide variety of extracellular bacterial proteins often in multiple tandem copies. (from Pfam)
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)
RTX calcium-binding repeat protein
cable pilus-associated adhesin AdhA
AdhA, a BafA-related non-fimbrial adhesin, works together with cable pili in Burkholderia to mediate binding to host cells. Most of roughly 3000 amino acid-long adhesin precursor consists of immunoglobulin-like repeats, each about 100 amino acids long.
type I secretion C-terminal target domain-containing protein
This model represents a C-terminal domain associated with secretion by type 1 secretion systems (T1SS). Members of this subclass do not include the RtxA toxin of Vibrio cholerae and its homologs, although the two classes of proteins share large size, occurrence in genomes with T1SS, regions with long tandem repeats, and regions with the glycine-rich repeat modeled by PF00353.
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.
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