cd02871, GH18_chitinase_D-like, GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus.
cd02871, GH18_chitinase_D-like, GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus.
pfam11712, Vma12, Endoplasmic reticulum-based factor for assembly of V-ATPase. The yeast vacuolar proton-translocating ATPase (V-ATPase) is the best characterized member of the V-ATPase family. A total of thirteen genes are required for encoding the subunits of the enzyme complex itself and an additional three for providing factors necessary for the assembly of the whole. Vma12 is one of these latter, all three of which are localized to the endoplasmic reticulum.
cd09608, M3B_PepF, Peptidase family M3B, oligopeptidase F (PepF). Peptidase family M3B oligopeptidase F (PepF; Pz-peptidase B; EC 3.4.24.-) is mostly bacterial and includes oligoendopeptidase F from Lactococcus lactis. This enzyme hydrolyzes peptides containing between 7 and 17 amino acids with fairly broad specificity. The PepF gene is duplicated in L. lactis on the plasmid that bears it, while a shortened second copy is found in Bacillus subtilis. Most bacterial PepFs are cytoplasmic endopeptidases; however, the Bacillus amyloliquefaciens PepF oligopeptidase is a secreted protein and may facilitate the process of sporulation. Specifically, the yjbG gene encoding the homolog of the PepF1 and PepF2 oligoendopeptidases of Lactococcus lactis has been identified in Bacillus subtilis as an inhibitor of sporulation initiation when over-expressed from a multicopy plasmid. This PepF family includes Streptococcus agalactiae PepB, a group B streptococcal oligopeptidase which has been shown to degrade a variety of bioactive peptides as well as the synthetic collagen-like substrate N-(3-[2-furyl]acryloyl)-Leu-Gly- Pro-Ala in vitro.
TIGR04547, putative_liporotein, MOLPALP family lipoprotein. Members of this family are surface lipoproteins, about 900 amino acids long on average, found only in the Mollicutes (Mycoplasma, Entomoplasma, Acholeplasma, Mesoplasma, Spiroplasma). Paralogs occur, such as MCAP_0360, MCAP_0361, and MCAP_0362 in Mycoplasma capricolum. This family shares significant N-terminal sequence similarity with STREFT (Secreted Thousand Residue Frequently Tandem), described by model TIGR04512; several members of the STREFT family have been misannotated as GnsA/GnsB family proteins. For proteins in this family, we suggest the name MOLPALP (Mollicutes Paralogous Lipoprotein) family lipoprotein [Cell envelope, Surface structures].
cd02871, GH18_chitinase_D-like, GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus.
cd02871, GH18_chitinase_D-like, GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus.
The bacterium proteins that are colored denote the protein is present at specific phage-related keywords (such as 'capsid', 'head', 'integrase', 'plate', 'tail', 'fiber', 'coat', 'transposase', 'portal', 'terminase', 'protease' or 'lysin' and 'tRNA')
