Protein data for LEXA_STRCO:

Description:
LexA repressor (EC 3.4.21.88).

Molecular weight: 25311

View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):

DNA repair( GO:0006281 )


Important dates:
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
07-MAR-2006, entry version 45.

Phylogenetic order:
Bacteria Actinobacteria Actinobacteridae Actinomycetales Streptomycineae Streptomycetaceae Streptomyces.

To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html

Links to references in other databases for protein LEXA_STRCO:

DatabasePointerAdd. info#1Add. info#2
EMBLAL939125CAA18339.1-
PIRT35123T35123.
HSSPP030331JHC
GenomeReviewsAL645882_GRSCO5803.1
BioCycSCOE1902:SCO5803-MONOMER-.1
HAMAPMF_00015-1.
InterProIPR006199LexA_DNA_bd.
InterProIPR006200Pept_S24_LexA.
InterProIPR006198Pept_S24_S26.
InterProIPR006197Pept_S24_SOS.
InterProIPR013324Sigma_r3_r4.
InterProIPR011991Wing_hlx_DNA_bd.
PfamPF01726LexA_DNA_bind1.
PfamPF00717Peptidase_S241.
PRINTSPR00726LEXASERPTASE.
TIGRFAMsTIGR00498lexA1.

General information about the databases mentioned above

Keywords:
Autocatalytic cleavage; Complete proteome; DNA damage; DNA repair; DNA replication; DNA-binding; Hydrolase; Repressor; SOS response; Transcription; Transcription regulation.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A3(2) / M145;
RX MEDLINE=21996410; PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
RA Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
RA Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
RA Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces
RT coelicolor A3(2).";
RL Nature 417:141-147(2002).

Feature:
CHAIN 1 234 LexA repressor.
/FTId=PRO_0000170096.
DNA_BIND 52 72 H-T-H motif (By similarity).
ACT_SITE 158 158 Involved in auto-cleavage (By
similarity).
ACT_SITE 195 195 Involved in auto-cleavage (By
similarity).
SITE 123 124 Cleavage (auto-) (By similarity).

Comments:
-!- FUNCTION: Represses a number of genes involved in the response to
DNA damage (SOS response), including recA and lexA. In the
presence of single-stranded DNA, recA interacts with lexA causing
an autocatalytic cleavage which disrupts the DNA-binding part of
lexA, leading to derepression of the SOS regulon and eventually
DNA repair (By similarity).
-!- CATALYTIC ACTIVITY: Hydrolysis of Ala-|-Gly bond in repressor
lexA.
-!- SUBUNIT: Homodimer (By similarity).
-!- SIMILARITY: Belongs to the peptidase S24 family.
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Sequence length: 234

     MSDAANPEGH KRSLPGRPPG IRADSSGLTD RQRRVIEVIR DSVQRRGYPP SMREIGQAVG
     LSSTSSVAHQ LMALERKGFL RRDPHRPRAY EVRGSDQAAS VQPTDTAGKP AASYVPLVGR
     IAAGGPILAE ESVEDVFPLP RQLVGDGELF VLKVVGDSMI EAAICDGDWV TVRRQPVAEN
     GDIVAAMLDG EATVKRFKRE DGHVWLLPHN SAYEPIPGDD ATILGKVVAV LRRV