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XprB

Protein FULL name:

xprB [Escherichia coli].


XprB (Escherichia coli strain K-12 substr. MG1655) is product of expression of xerD gene.






FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds cooperatively to specific DNA consensus sequences that are separated from xerC binding sites by a short central region, forming the heterotetrameric xerC-xerD complex that recombines DNA substrates. The complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids at ColE1 xer (or cer) and pSC101 (or psi) sites. In the complex xerD specifically exchanges the bottom DNA strands (By similarity).

ENZYME REGULATION: During recombination, the heterotetrameric complex catalyzes two consecutive pairs of strand exchanges, implying that specific pairs of active sites are sequentially switched on and off in the recombinase tetramer to ensure that appropriate DNA strands will be exchanged at both reaction steps. FtsK plays a central role in this catalytic state switch that turns recombinase on and off reciprocally. The reciprocal C- terminal interaction between xerC and xerD may also participate in the enzymatic switch process.

SUBUNIT: Forms a cyclic heterotetrameric complex composed of two molecules of xerC and two molecules of xerD, in which xerC interacts with xerD via its C-terminal region, xerD interacts with xerC via its C-terminal region and so on.

SUBCELLULAR LOCATION: Cytoplasm (By similarity).

SIMILARITY: Belongs to the 'phage' integrase family. XerD subfamily.


NCBI GenPept GI number(s): 147548
Species: Escherichia coli

Links to other databases:

Database ID Link
Uniprot P0A8P8 P0A8P8
PFAM: - P0A8P8 (Link - using uniprot id)
InterPro: - P0A8P8 (Link - using uniprot id)
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MKQDLARIEQFLDALWLEKNLAENTLNAYRRDLSMMVEWLHHRGLTLATA
QSDDLQALLAERLEGGYKATSSARLLSAVRRLFQYLYREKFREDDPSAHL
ASPKLPQRLPKDLSEAQVERLLQAPLIDQPLELRDKAMLEVLYATGLRVS
ELVGLTMSDISLRQGVVRVIGKGNKERLVPLGEEAVYWLETYLEHGRPWL
LNGVSIDVLFPSQRAQQMTRQTFWHRIKHYAVLAGIDSEKLSPHVLRHAF
ATHLLNHGADLRVVQMLLGHSDLSTTQIYTHVATERLRQLHQQHHPRA

XprB (Escherichia coli strain K-12 substr. MG1655) is able to recognize following damages:
References:

Title Authors Journal
Nucleotide sequence of the Escherichia coli recJ chromosomal region and construction of recJ-overexpression plasmids. Lovett ST, Kolodner RD J Bacteriol Feb. 1, 1991
Two related recombinases are required for site-specific recombination at dif and cer in E. coli K12. Blakely G, May G, McCulloch R, Arciszewska LK, Burke M, Lovett ST, Sherratt DJ Cell Oct. 22, 1993
Xer site-specific recombination in vitro. Arciszewska LK, Sherratt DJ EMBO J May 1, 1995
Xer recombination in Escherichia coli. Site-specific DNA topoisomerase activity of the XerC and XerD recombinases. Cornet F, Hallet B, Sherratt DJ J Biol Chem Aug. 1, 1997
Crystal structure of the site-specific recombinase, XerD. Subramanya HS, Arciszewska LK, Baker RA, Bird LE, Sherratt DJ, Wigley DB EMBO J Sept. 1, 1997
The complete genome sequence of Escherichia coli K-12. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y Science Sept. 5, 1997
C-terminal interactions between the XerC and XerD site-specific recombinases. Spiers AJ, Sherratt DJ Mol Microbiol June 1, 1999
Reciprocal control of catalysis by the tyrosine recombinases XerC and XerD: an enzymatic switch in site-specific recombination. Hallet B, Arciszewska LK, Sherratt DJ Mol Cell Dec. 1, 1999
FtsK Is a DNA motor protein that activates chromosome dimer resolution by switching the catalytic state of the XerC and XerD recombinases. Aussel L, Barre FX, Aroyo M, Stasiak A, Stasiak AZ, Sherratt D Cell Feb. 25, 2002
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T Mol Syst Biol Jan. 1, 2006


Last modification of this entry: Oct. 6, 2010.

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