Protein Family Models

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)

Date:

2024-10-16

PplA, as found in extracellular electron transfer (EET) locus of Listeria monocytogenes, is a cell surface flavoprotein with covalently attached FMN. Flavinylation is performed by FmnB, a family ApbE surface lipoprotein, using FAD as the source molecule. This HMM describes a long form of PplA, with a duplication of the flavinylated domain and with two bound FMN molecules.

Gene:

pplA

Date:

2023-07-24