Nucleotide-binding domain of HSPA12A, HSPA12B and similar proteins. Human HSPA12A (also known as 70-kDa heat shock protein-12A) and HSPA12B (also known as 70-kDa heat shock protein-12B, chromosome 20 open reading frame 60/C20orf60, dJ1009E24.2) belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A or HSPA12B. The gene encoding HSPA12A maps to 10q26.12, a cytogenetic region that might represent a common susceptibility locus for both schizophrenia and bipolar affective disorder; reduced expression of HSPA12A has been shown in the prefrontal cortex of subjects with schizophrenia. HSPA12A is also a candidate gene for forelimb-girdle muscular anomaly, an autosomal recessive disorder of Japanese black cattle. HSPA12A is predominantly expressed in neuronal cells. It may also play a role in the atherosclerotic process. The gene encoding HSPA12B maps to 20p13. HSPA12B is predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. HSPA12B expression is up-regulated in lipopolysaccharide (LPS)-induced inflammatory response in the spinal cord, and mostly located in active microglia; this induced expression may be regulated by activation of MAPK-p38, ERK1/2 and SAPK/JNK signaling pathways. Overexpression of HSPA12B also protects against LPS-induced cardiac dysfunction and involves the preserved activation of the PI3K/Akt signaling pathway.

Glycosyltransferases, probably involved in cell wall biogenesis [Cell envelope biogenesis, outer membrane]

Nucleotide-binding domain of HSPA12A, HSPA12B and similar proteins. Human HSPA12A (also known as 70-kDa heat shock protein-12A) and HSPA12B (also known as 70-kDa heat shock protein-12B, chromosome 20 open reading frame 60/C20orf60, dJ1009E24.2) belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A or HSPA12B. The gene encoding HSPA12A maps to 10q26.12, a cytogenetic region that might represent a common susceptibility locus for both schizophrenia and bipolar affective disorder; reduced expression of HSPA12A has been shown in the prefrontal cortex of subjects with schizophrenia. HSPA12A is also a candidate gene for forelimb-girdle muscular anomaly, an autosomal recessive disorder of Japanese black cattle. HSPA12A is predominantly expressed in neuronal cells. It may also play a role in the atherosclerotic process. The gene encoding HSPA12B maps to 20p13. HSPA12B is predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. HSPA12B expression is up-regulated in lipopolysaccharide (LPS)-induced inflammatory response in the spinal cord, and mostly located in active microglia; this induced expression may be regulated by activation of MAPK-p38, ERK1/2 and SAPK/JNK signaling pathways. Overexpression of HSPA12B also protects against LPS-induced cardiac dysfunction and involves the preserved activation of the PI3K/Akt signaling pathway.

cellulose synthase catalytic subunit (UDP-forming). Cellulose synthase catalyzes the beta-1,4 polymerization of glucose residues in the formation of cellulose. In bacteria, the substrate is UDP-glucose. The synthase consists of two subunits (or domains in the frequent cases where it is encoded as a single polypeptide), the catalytic domain modelled here and the regulatory domain (pfam03170). The regulatory domain binds the allosteric activator cyclic di-GMP. The protein is membrane-associated and probably assembles into multimers such that the individual cellulose strands can self-assemble into multi-strand fibrils.

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose. Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.