Beta- N-acetylglucosaminidase [Carbohydrate transport and metabolism].

Type I dockerin repeat domain. Bacterial cohesin domains bind to a complementary protein domain named dockerin, and this interaction is required for the formation of the cellulosome, a cellulose-degrading complex. The cellulosome consists of scaffoldin, a noncatalytic scaffolding polypeptide, that comprises repeating cohesion modules and a single carbohydrate-binding module (CBM). Specific calcium-dependent interactions between cohesins and dockerins appear to be essential for cellulosome assembly. This subfamily represents type I dockerins, which are responsible for anchoring a variety of enzymatic domains to the complex.

Dockerin type I repeat. The dockerin repeat is the binding partner of the cohesin domain pfam00963. The cohesin-dockerin interaction is the crucial interaction for complex formation in the cellulosome. The dockerin repeats, each bearing homology to the EF-hand calcium-binding loop bind calcium.

Cadherin-like beta sandwich domain. This domain is found in several bacterial, metazoan and chlorophyte algal proteins. A profile-profile comparison recovered the cadherin domain and a comparison of the predicted structure of this domain with the crystal structure of the cadherin showed a congruent seven stranded secondary structure. The domain is widespread in bacteria and seen in the firmicutes, actinobacteria, certain proteobacteria, bacteroides and chlamydiae with an expansion in Clostridium. In contrast, it is limited in its distribution in eukaryotes suggesting that it was derived through lateral transfer from bacteria. In prokaryotes, this domain is widely fused to other domains such as FNIII (Fibronectin Type III), TIG, SLH (S-layer homology), discoidin, cell-wall-binding repeat domain and alpha-amylase-like glycohydrolases. These associations are suggestive of a carbohydrate-binding function for this cadherin-like domain. In animal proteins it is associated with an ATP-grasp domain.

Dockerin repeat domains and domains resembling dockerin repeats. Dockerins are modules in the cellulosome complex that often anchor catalytic subunits by binding to cohesin domains of scaffolding proteins. Three types of dockerins and their corresponding cohesin have been described in the literature. This alignment models two consecutive dockerin repeats, the functional unit.

ChainA, Bifunctional autolysin [Staphylococcus aureus subsp. aureus Mu50]

ChainA, Uncharacterized protein [Staphylococcus aureus subsp. aureus Mu50],6FXP_B Chain B, Uncharacterized protein [Staphylococcus aureus subsp. aureus Mu50]

ChainB, LYZ2 domain-containing protein [Staphylococcus aureus subsp. aureus NCTC 8325]

Bifunctional autolysin OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=atl PE=3 SV=1

Bifunctional autolysin OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=atl PE=3 SV=1

Bifunctional autolysin OS=Staphylococcus epidermidis OX=1282 GN=atl PE=1 SV=1

Bifunctional autolysin OS=Staphylococcus aureus (strain COL) OX=93062 GN=atl PE=3 SV=1

Bifunctional autolysin OS=Staphylococcus aureus (strain MW2) OX=196620 GN=atl PE=3 SV=1