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ABC transporter permease subunit
The alignments cover the most conserved region of the proteins, which is thought to be located in a cytoplasmic loop between two transmembrane domains. The members of this family have a variable number of transmembrane helices. (from Pfam)
ABC transporter permease
ABC transporter permease is the transmembrane subunit found in a periplasmic binding protein (PBP)-dependent ABC transport system, which may be involved in the transport of one or more from a variety of substrates including sugars, ions, amino acids, and peptides, among others
molybdate ABC transporter permease subunit
This HMM describes the permease protein, ModB, of the molybdate ABC transporter. This system has been characterized in E. coli [1], Staphylococcus carnosus [2] Rhodobacter capsulatus [3] and Azotobacter vinlandii [4]. Molybdate is chemically similar to sulfate, thiosulfate, and selenate. These related substrates, and sometimes molybdate itself, can be transported by the homologous sulfate receptor. Some apparent molybdenum transport operons include a permease related to this ModB, although less similar than some sulfate permease proteins and not included in this model.
This model describes a clade of ABC porter genes with relatively weak homology compared to its neighbor clades, the molybdate (TIGR02141) and sulfate (TIGR00969) porters. Neighbor-Joining, PAM-distance phylogenetic trees support the separation of the clades in this way. Included in this group is a gene designated NifC in Clostridium pasturianum [1]. It would be reasonable to presume that NifC acts as a molybdate porter since the most common form of nitrogenase is a molybdoenzyme. Several other sequences falling within the scope of this model are annotated as molybdate porters and one, from Halobacterium, is annotated as a sulfate porter. There is presently no experimental evidence to support annotations with this degree of specificity.
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