Efflux transporter (ATP-binding and permease protein); An efflux transporter able to transport Hoechst 33342, ethidium bromide, doxorubicin and a number of other drugs in vitro into inside out vesicles. The endogenous substrate is unknown. It has been suggested that NBD dimerization induced by ATP-binding causes a large conformational change responsible for substrate translocation. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable).

Multidrug-efflux transporter; Energy-dependent efflux pump responsible for decreased drug accumulation in multi-drug-resistant cells. Probably uses a transmembrane proton gradient as the energy source. Causes the efflux of a variety of toxic substances, including such structurally diverse compounds as ethidium bromide, rhodamine and acridine dyes, tetraphenylphosphonium, puromycin, chloramphenicol, doxorubicin, and fluoroquinolone antibiotics; Belongs to the major facilitator superfamily. TCR/Tet family.

MatE Na+-driven efflux family protein; Multidrug efflux pump; Belongs to the multi antimicrobial extrusion (MATE) (TC 2.A.66.1) family.

L-asparaginase 2 (putative lipoprotein); Catalyzes the conversion of L-asparagine to L-aspartate and ammonium.

Quercetin dioxygenase; Performs the first step in the degradation of the flavonoid quercetin by a dioxygenase reaction. The enzyme catalyzes the cleavage of the O-heteroaromatic ring of the flavonol quercetin yielding the depside 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon monoxide. This involves the remarkable dioxygenolytic cleavage of two carbon-carbon bonds.

Manganese ABC transporter (manganese binding lipoprotein); Probably part of the ABC transporter complex MntABCD involved in manganese import.

Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.

ATP-binding tunicamycin resistance protein; Involved in the resistance to tunicamycin. Binds ATP.