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Literature summary for 2.7.8.B10 extracted from

  • Romantsov, T.; Gonzalez, K.; Sahtout, N.; Culham, D.E.; Coumoundouros, C.; Garner, J.; Kerr, C.H.; Chang, L.; Turner, R.J.; Wood, J.M.
    Cardiolipin synthase A colocalizes with cardiolipin and osmosensing transporter ProP at the poles of Escherichia coli cells (2018), Mol. Microbiol., 107, 623-638 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
molecular modeling of structure Escherichia coli

Protein Variants

Protein Variants Comment Organism
H224A/H404A mutations inactivate ClsA and compromise transporter ProP localization Escherichia coli

Localization

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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification ClsA is N-terminally processed Escherichia coli

Subunits

Subunits Comment Organism
? x * 54822, calculated from sequence, x * 46000, SDS-PAGE Escherichia coli

General Information

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