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FMN-binding protein
This conserved region includes the FMN-binding site of the NqrC protein [1] as well as the NosR and NirI regulatory proteins. This domain is post-translationally flavinylated that may facilitate electron transfer, and thus, resembles multiheme cytochromes [3]. [1]. 11248234. Expression and mutagenesis of the NqrC subunit of the NQR respiratory Na(+) pump from Vibrio cholerae with covalently attached FMN. Barquera B, Hase CC, Gennis RB;. FEBS Lett 2001;492:45-49. [2]. 12625841. New Knowledge from Old: In silico discovery of novel protein domains in Streptomyces coelicolor. Yeats C, Bentley S, Bateman A;. BMC Microbiol 2003;3:3-3. [3]. 34032212. Post-translational flavinylation is associated with diverse extracytosolic redox functionalities throughout bacterial life. Meheust R, Huang S, Rivera-Lugo R, Banfield JF, Light SH;. Elife. 2021; [Epub ahead of print] (from Pfam)
NADH:ubiquinone reductase (Na(+)-transporting) subunit C
This HMM represents the NqrC subunit of the six-protein, Na(+)-pumping NADH-quinone reductase of a number of marine and pathogenic Gram-negative bacteria. This oxidoreductase complex functions primarily as a sodium ion pump [1].
Na+-translocating NADH-quinone reductase subunit C
Na(+)-translocating NADH-quinone reductase subunit C is part of the Na(+)-NQR complex that couples the respiratory chain to ion translocation across the membrane in order to build up an electrochemical gradient
Na(+)-translocating NADH-quinone reductase subunit C
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