| UniProt functional annotation for P46084 | |||
| UniProt codes: P0DPR0, P46084. |
| Organism: | Clostridium botulinum C phage (Clostridium botulinum C bacteriophage). | |
| Taxonomy: | Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; Caudovirales; Siphoviridae. | |
| Function: | Agglutinates human erythrocytes (PubMed:2205574). The hemagglutinin (HA) component of the progenitor toxin protects the structural integrity of botulinum neurotoxin; may increase internalization of the neurotoxin into the bloodstream of the host (PubMed:9421908). The hemagglutinin (HA) component is involved in binding to the upper small intestine through interactions with glycolipids and glycoproteins containing sialic acid moieties (Probable). Binds galactose or oligosaccharides with galactose at their non-reducing end (PubMed:14663070). Binds eukaryotic host mucins; binding is inhibited by N-acetyl-beta-neuraminic acid, N-acetyl-D- galactosamine, galactose, and methyl N-acetyl-beta-neuraminic acid (PubMed:18178224). Binds N-acetyl-beta-neuraminic acid, N-acetyl-D- galactosamine and galactose (but not glucose) via 2 sites (PubMed:18178224, PubMed:21640703). {ECO:0000269|PubMed:14663070, ECO:0000269|PubMed:18178224, ECO:0000269|PubMed:21640703, ECO:0000269|PubMed:2205574, ECO:0000269|PubMed:9421908, ECO:0000305|PubMed:9421908}. | |
| Subunit: | Botulinum toxins are produced as progenitor toxins of large molecular sizes of 12S (M toxin) and 16S (L toxin). M toxin consists of a non-toxic, non-hemagglutinin component (NTNHA) and the neurotoxin (Probable). L toxin consists of the M toxin and the 3 subcomponents of hemagglutinin (HA) (PubMed:7802661). HA is composed of subcomponents of 70, 33, and 17 kDa (PubMed:7802661). The 70 kDa subcomponent undergoes proteolytic processing and is split into HA-55 (also called HA-53 and HA3b) and HA-22-23 (also called HA3a) (PubMed:7802661). The stoichiometry of the whole complex has been modeled as one BoNT/C, one NTNHA, three HA-70, six HA-33 and three HA-17 (By similarity). {ECO:0000250|UniProtKB:P0DPR1, ECO:0000269|PubMed:7802661, ECO:0000305|PubMed:7802661}. | |
| Subcellular location: | Secreted {ECO:0000269|PubMed:2205574, ECO:0000269|PubMed:7802661}. | |
| Domain: | Arranged in 2 beta-trefoil domains (called 1 and 2) each with three tandemly repeated subdomains (called alpha, beta and gamma) joined by a short alpha-helix (Probable). Only subdomains 2-alpha and 2-gamma, in the C-terminal beta-trefoil domain, possess a functional carbohydrate-binding site (PubMed:18178224, PubMed:21640703). {ECO:0000269|PubMed:18178224, ECO:0000269|PubMed:21640703, ECO:0000305|PubMed:14663070, ECO:0000305|PubMed:18178224, ECO:0000305|PubMed:21640703}. | |
| Miscellaneous: | This protein can also be encoded on a prophage. {ECO:0000305}. | |
Annotations taken from UniProtKB at the EBI.