Protein Family Models

This domain is found at the C-terminal of FakA (fatty acid subunit A) proteins, which is part of the fatty acid kinase machinery [1]. In the human pathogens Staphylococcus and Streptococcus, this system is used to scavenge host fatty acids. FakA is an ATP-binding subunit which interacts with varied FakB (fatty acid-binding protein) isoforms and synthesises acyl-phosphate from extracellular fatty acids [1]. FakA comprises three domains (FakA_N, FakA_M and FakA_C) and resembles an evolutionary mimic of the DhaK-DhaL kinase system. This entry represents FakA_C, which acts as a recipient of fatty acids transferred from FakB in the context of Fak activity [1]. [1]. 36054360. Structure and mechanism for streptococcal fatty acid kinase. (Fak) system dedicated to host fatty acid scavenging.. Shi Y, Zang N, Lou N, Xu Y, Sun J, Huang M, Zhang H, Lu H, Zhou. C, Feng Y;. Sci Adv. 2022;8:eabq3944. (from Pfam)

Date:

2024-08-14

The structure of this protein revealed a bound fatty-acid molecule in a pocket between the two protein domains. The structure indicates that this family has the molecular function of fatty-acid binding and may play a role in the cellular functions of fatty acid transport or metabolism [1]. [1]. 12577257. Crystal structure of a hypothetical protein, TM841 of Thermotoga. maritima, reveals its function as a fatty acid-binding protein.. Schulze-Gahmen U, Pelaschier J, Yokota H, Kim R, Kim SH;. Proteins 2003;50:526-530. (from Pfam)

Date:

2024-08-14

FakB1 and FakB2 are two homologs of the DegV protein family (COG1307). Incubation of FakB2 with FakA (fatty acid kinase FakA) leds to the formation of acyl phosphates from fatty acids. Analysis of the substrate preference of the FakB1 and FakB2 showed that FakB1 preferred saturated fatty acids, whereas FakB2 preferred unsaturated acids, with a strong preference for oleate.

Gene:

fakB2

Date:

2020-12-17

DegV family protein similar to Bacillus subtilis DegV, which binds long-chain fatty acids such as palmitate, and may play a role in lipid transport or fatty acid metabolism

Date:

2022-08-17

This family of proteins is related to DegV of Bacillus subtilis and includes paralogous sets in several species (B. subtilis, Deinococcus radiodurans, Mycoplasma pneumoniae) that are closer in percent identity to each than to most homologs from other species. This suggests both recent paralogy and diversity of function. DegV itself is encoded immediately downstream of DegU, a transcriptional regulator of degradation, but is itself uncharacterized. Crystallography suggested a lipid-binding site, while comparison of the crystal structure to dihydroxyacetone kinase and to a mannose transporter EIIA domain suggests a conserved domain, EDD, with phosphotransferase activity.

Date:

2024-08-07