Crystallization (Comment) | Organism |
---|---|
molecular modeling of structure | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
H224A/H404A | mutations inactivate ClsA and compromise transporter ProP localization | Escherichia coli |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cell pole | - |
Escherichia coli | 60187 | - |
membrane | ClsA is membrane-anchored, with dual, cytoplasmic, catalytic domains | Escherichia coli | 16020 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | ClsA is N-terminally processed | Escherichia coli |
Subunits | Comment | Organism |
---|---|---|
? | x * 54822, calculated from sequence, x * 46000, SDS-PAGE | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
physiological function | ClsA and proteins YdhP, YjbJ interact with transporter ProP. All three proteins are concentrated at the cell poles, but only ClsA localization was cardiolipin-dependent. ClsA is N-terminally processed and membrane-anchored, with dual, cytoplasmic, catalytic domains | Escherichia coli |