Accession | TIGR00147 |
Name | TIGR00147 |
Function | lipid kinase, YegS/Rv2252/BmrU family |
Trusted Cutoff | 118.65 |
Domain Trusted Cutoff | 118.65 |
Noise Cutoff | 102.30 |
Domain Noise Cutoff | 102.30 |
Isology Type | subfamily |
EC Number | 2.7.1.- |
HMM Length | 296 |
Mainrole Category | Unknown function |
Subrole Category | Enzymes of unknown specificity |
Gene Ontology Term | GO:0001727: lipid kinase activity molecular_function |
| GO:0005575: cellular_component cellular_component |
| GO:0008150: biological_process biological_process |
Author | Richardson DL, Haft DH |
Entry Date | Apr 20 1999 2:05PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | The E. coli member of this family, YegS has been purified [1] and shown to have phosphatidylglycerol kinase activity. The member from M. tuberculosis, Rv2252, has diacylglycerol kinase activity. BmrU from B. subtilis is in an operon with multidrug efflux transporter Bmr, but is uncharacterized. |
References | SE TIGR
DR HAMAP; MF_01377; 40 of 41
RN [1]
RM PMID:17351295
RT Crystal structure of YegS, a homologue to the mammalian diacylglycerol kinases, reveals a novel regulatory metal binding site.
RA Bakali HM, Herman MD, Johnson KA, Kelly AA, Wieslander A, Hallberg BM, Nordlund P
RL J Biol Chem. 2007 Jul 6;282(27):19644-52. Epub 2007 Mar 11.
RN [2]
RM PMID:10220166
RT Identification and transcriptional analysis of new members of the sigmaB regulon in Bacillus subtilis.
RA Petersohn A, Antelmann H, Gerth U, Hecker M
RL Microbiology. 1999 Apr;145 ( Pt 4):869-80.
RN [3]
RM PMID:7961792
RT A protein that activates expression of a multidrug efflux transporter upon binding the transporter substrates.
RA Ahmed M, Borsch CM, Taylor SS, Vazquez-Laslop N, Neyfakh AA
RL J Biol Chem. 1994 Nov 11;269(45):28506-13. |