| Accession | TIGR00750 |
| Name | lao |
| Function | LAO/AO transport system ATPase |
| Trusted Cutoff | 240.75 |
| Domain Trusted Cutoff | 240.75 |
| Noise Cutoff | 157.75 |
| Domain Noise Cutoff | 157.75 |
| Isology Type | equivalog |
| EC Number | 2.7.-.- |
| HMM Length | 300 |
| Mainrole Category | Transport and binding proteins |
| Subrole Category | Amino acids, peptides and amines |
| Gene Ontology Term | GO:0015809: arginine transport biological_process |
| | GO:0015819: lysine transport biological_process |
| | GO:0015822: ornithine transport biological_process |
| | GO:0016772: transferase activity, transferring phosphorus-containing groups molecular_function |
| Author | Loftus BJ, Haft DH |
| Entry Date | Mar 2 2000 2:33PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | In E. coli, mutation of this kinase blocks phosphorylation of two transporter system periplasmic binding proteins and consequently inhibits those transporters. This kinase is also found in Gram-positive bacteria, archaea, and the roundworm C. elegans. It may have a more general, but still unknown function.
Mutations have also been found that do not phosphorylate the periplasmic binding proteins, yet still allow transport. The ATPase activity of this protein seems to be necessary, however. |
| References | SE
AL clustalw_manual
A2 hmmalign
SE COG/EC_num
RN [1]
RM 90110251
RT Purification and properties of a kinase from Escherichia coli K-12 that phosphorylates two periplasmic transport proteins.
RA Urban C, Celis RT
RL J Biol Chem 1990 Jan 25;265(3):1783-6
RN [2]
RM 90110252
RT Mutant of Escherichia coli K-12 with defective phosphorylation of two periplasmic transport proteins.
RA Celis RT
RL J Biol Chem 1990 Jan 25;265(3):1787-93 |
