Accession | TIGR01689 |
Name | EcbF-BcbF |
Function | capsule biosynthesis phosphatase |
Trusted Cutoff | 162.00 |
Domain Trusted Cutoff | 162.00 |
Noise Cutoff | 47.80 |
Domain Noise Cutoff | 47.80 |
Isology Type | subfamily |
HMM Length | 126 |
Author | Selengut J |
Entry Date | Sep 20 2002 2:20PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | This model describes a small family of highly conserved proteins (>60% ID). Two of these, BcbF and EcbF of Pasteurella multocida are believed to be part of the capsule polysaccharide biosynthesis machinery because they are cotranscribed from a locus devoted to that purpose [1]. In pasteurella there are six different variant capsules (A-F), and these proteins are found only in B and E. The other two species in which this gene is (currently) found are both also pathogenic.
These proteins are also members of the IIIC (TIGR01681) subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. All of the characterized enzymes within subfamily III are phosphatases, and all of the active site residues characteristic of HAD-superfamily phosphatases [2] are present in this subfamily.
Due to the likelihood that the substrates of these enzymes are different depending on the nature of the particular polysaccharides associated with each species, this model has been classified as a subfamily despite the close homology. |
References | RN [1]
RM PMID: 10699509
RT Genetic organisation of the capsule biosynthetic locus of Pasteurella multocida M1404 (B:2).
RA Boyce JD, Chung JY, Adler B.
RL Vet Microbiol 2000 Mar 1;72(1-2):121-34
RN [2]
RM PMID: 7966317
RT Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search.
RA Koonin EV, Tatusov RL.
RL J Mol Biol 1994 Nov 18;244(1):125-32 |