Tracing the spread of fibronectin type III domains in bacterial glycohydrolases

Little, Elizabeth; Bork, Peer; Doolittle, Russell F.

doi:10.1007/bf00160409

Cited by 112 publications

(91 citation statements)

References 49 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…We have detected these domains based solely on sequence similarities, and thus feel confident drawing a conclusion of divergent evolution. However, we cannot dismiss, at present, the possibility that these Ig domains were acquired horizontally by prokaryotes from eukaryotes after their divergence [as has been proposed for the bacterial examples of the fibronectin type 111 domain (Bork & Doolittle, 1992; Little et al, 1994)] rather than their being the descendants of a true bacterial ancestor of the Ig superfamily.…”

Section: Rhqvtttk-----ykstfeissvqasdegnyswvens-egkq-eaeftltiqmentioning

confidence: 88%

See 1 more Smart Citation

Members of the immunoglobulin superfamily in bacteria

1996

View full text Add to dashboard Cite

Abstract:We report a prediction that two prokaryotic proteins contain immunoglobulin superfamily domains. Immunoglobulinlike folds have been identified previously in prokaryotic proteins, but these share no recognizable sequence similarity with eukaryotic immunoglobulin superfamily (IgSF) folds, and may be the result of the physics and chemistry of proteins favoring certain common folds. In contrast, the prokaryotic proteins identified have sequences whose match to the immunoglobulin superfamily can be detected by hidden Markov modeling, BLASTP matches, key residue analysis, and secondary structure predictions. We propose that these prokaryotic immunoglobulin-like domains are almost certain to be related by divergence from a common ancestor to eukaryotic immunoglobulin superfamily domains.

show abstract

Section: Rhqvtttk-----ykstfeissvqasdegnyswvens-egkq-eaeftltiqmentioning

confidence: 88%

“…The function of the region containing the Ig-like domains is unknown (Coutinho et al, 1992). Endoglucanases B and D from C. fimi contain fibronectin type I11 domains, which have an immunoglobulin-like fold, but there is no evidence that these domains are members of the IgSF (Little et al, 1994).…”

mentioning

confidence: 99%

Members of the immunoglobulin superfamily in bacteria

1996

View full text Add to dashboard Cite

show abstract

“…FnIII-like domains are widely distributed among family 18 bacterial chitinases and other glycosyl hydrolases (Little et al, 1994), but have not been reported for any family 19 chitinases (CAZy, 2013;Punta et al, 2012). They appear to contribute to chitin hydrolysis (Watanabe et al, 1994), possibly by functioning as a flexible linker between the catalytic and chitin-binding domain (Jee et al, 2002).…”

Section: Functional Roles Of Other Accessory Modulesmentioning

confidence: 99%

Bacterial chitinases and chitin-binding proteins as virulence factors

et al. 2013

View full text Add to dashboard Cite

“…The bacterial Fn3 domain was first identified in chitinase A1 of B. circulans WL-12 [36] and was later found in many bacterial enzymes such as chitinases, cellulases, amylases and poly(3-hydroxybutyrate) depolymerases [37]. Among bacterial enzymes degrading insoluble substrates, the Fn3 domains have been most frequently found in chitinases.…”

Section: Multidomain Structure Of Chitinase C1mentioning

confidence: 99%

The third chitinase gene (chiC) of Serratia marcescens 2170 and the relationship of its product to other bacterial chitinases

Suzuki

Taiyoji

Sato

et al. 1999

Biochemical Journal

142

123

View full text Add to dashboard Cite

The third chitinase gene (chiC) of Serratia marcescens 2170, specifying chitinases C1 and C2, was identified. Chitinase C1 lacks a signal sequence and consists of a catalytic domain belonging to glycoside hydrolase family 18, a fibronectin type III-like domain (Fn3 domain) and a C-terminal chitin-binding domain (ChBD). Chitinase C2 corresponds to the catalytic domain of C1 and is probably generated by proteolytic removal of the Fn3 and ChBDs. The loss of the C-terminal portion reduced the hydrolytic activity towards powdered chitin and regenerated chitin, but not towards colloidal chitin and glycol chitin, illustrating the importance of the ChBD for the efficient hydrolysis of crystalline chitin. Phylogenetic analysis showed that bacterial family 18 chitinases can be clustered in three subfamilies which have diverged at an early stage of bacterial chitinase evolution. Ser. marcescens chitinase C1 is found in one subfamily, whereas chitinases A and B of the same bacterium belong to another subfamily. Chitinase C1 is the only Ser. marcescens chitinase that has an Fn3 domain. The presence of multiple, divergent, chitinases in a single chitinolytic bacterium is perhaps necessary for efficient synergistic degradation of chitin.

show abstract

Tracing the spread of fibronectin type III domains in bacterial glycohydrolases

Cited by 112 publications

References 49 publications

Members of the immunoglobulin superfamily in bacteria

Members of the immunoglobulin superfamily in bacteria

Bacterial chitinases and chitin-binding proteins as virulence factors

The third chitinase gene (chiC) of Serratia marcescens 2170 and the relationship of its product to other bacterial chitinases

Contact Info

Product

Resources

About