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porin
This family consists of porins from the alpha subdivision of Proteobacteria the members of this family are related to Pfam:PF00267. The porins form large aqueous channels in the cell membrane allowing the selective entry of hydrophilic compounds this so called 'molecular sieve' is found in the cell walls of gram negative bacteria. (from Pfam)
outer membrane protein transport protein
This family includes TodX from Pseudomonas putida F1 Swiss:Q51971 and TbuX from Ralstonia pickettii PKO1 Swiss:Q9RBW8. These are membrane proteins of uncertain function that are involved in toluene catabolism. Related proteins involved in the degradation of similar aromatic hydrocarbons are also in this family, such as CymD Swiss:O33458. This family also includes FadL involved in translocation of long-chain fatty acids across the outer membrane. It is also a receptor for the bacteriophage T2. [1]. 7535376. Identification of a membrane protein and a truncated LysR-type regulator associated with the toluene degradation pathway in Pseudomonas putida F1. Wang Y, Rawlings M, Gibson DT, Labbe D, Bergeron H, Brousseau R, Lau PC;. Mol Gen Genet 1995;246:570-579. [2]. 10671442. Characterization and role of tbuX in utilization of toluene by Ralstonia pickettii PKO1. Kahng HY, Byrne AM, Olsen RH, Kukor JJ;. J Bacteriol 2000;182:1232-1242. [3]. 9150211. p-Cymene catabolic pathway in Pseudomonas putida F1: cloning and characterization of DNA encoding conversion of p-cymene to p-cumate. Eaton RW;. J Bacteriol 1997;179:3171-3180. (from Pfam)
OmpP1/FadL family transporter
OmpP1/FadL family protein similar to Haemophilus influenzae outer membrane protein P1 and Escherichia coli long-chain fatty acid transporter FadL, which is responsible for the transport of hydrophobic compounds across the bacterial outer membrane
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