|PROSITE documentation PDOC00131 [for PROSITE entry PS50163]|
The bacterial recA protein [1,2,3] is essential for homologous recombination and recombinational repair of DNA damage. RecA has many activities: it filaments, it binds to single- and double-stranded DNA, it binds and hydrolyzes ATP, it is also a recombinase and, finally, it interacts with lexA causing its activation and leading to its autocatalytic cleavage.
The recA protein is closely related to:
As a signature pattern specific for the bacterial and chloroplastic recA protein, we selected the best conserved region, a nonapeptide located in the middle of the sequence and which is part of the monomer-monomer interface in a recA filament.
We also developed two profiles. The first one covers the ATP binding domain in the N-terminal part of the recA protein. The second one span the whole monomer-monomer interface. These two profiles also pick up the recA-like proteins.
Eisen J.A.; email@example.comExpert(s) to contact by email:
Roca A.I.;Last update:
December 2012 / Profile revised.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Smith K.C., Wang T.-C.|
|Title||recA-dependent DNA repair processes.|
|2||Authors||Lloyd A.T., Sharp P.M.|
|Title||Evolution of the recA gene and the molecular phylogeny of bacteria.|
|Source||J. Mol. Evol. 37:399-407(1993).|
|3||Authors||Roca A.I., Cox M.M.|
|Source||Prog. Nucleic Acids Res. Mol. Biol. 56:129-223(1997).|
|4||Authors||Karlin S., Weinstock G.M., Brendel V.|
|Title||Bacterial classifications derived from recA protein sequence comparisons.|
|Source||J. Bacteriol. 177:6881-6893(1995).|
|Title||The RecA protein as a model molecule for molecular systematic studies of bacteria: comparison of trees of RecAs and 16S rRNAs from the same species.|
|Source||J. Mol. Evol. 41:1105-1123(1995).|
|6||Authors||Cerutti H.D., Osman M., Grandoni P., Jagendorf A.T.|
|Title||A homolog of Escherichia coli RecA protein in plastids of higher plants.|
|Source||Proc. Natl. Acad. Sci. U.S.A. 89:8068-8072(1992).|