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Protein data for LEXA_DEIRA:

Description:
LexA repressor (EC 3.4.21.88).

Molecular weight: 22351

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:
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
07-MAR-2006, entry version 45.

Phylogenetic order:
Bacteria Deinococcus-Thermus Deinococci Deinococcales Deinococcaceae Deinococcus.

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_DEIRA:

DatabasePointerAdd. info#1Add. info#2
EMBLAB003475BAA21376.1-
EMBLAE001825AAF12438.1ALT_INIT
HSSPP030331JHC
GenomeReviewsAE001825_GRDRA0344.1
TIGRDRA0344-.
HAMAPMF_00015-1.
InterProIPR001845HTH_ArsR.
InterProIPR006200Pept_S24_LexA.
InterProIPR006198Pept_S24_S26.
InterProIPR006197Pept_S24_SOS.
InterProIPR011991Wing_hlx_DNA_bd.
PfamPF01022HTH_51.
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 [GENOMIC DNA].
RC STRAIN=KD8301;
RA Narumi I., Kong X., Du Z., Cherdchu K., Kitayama S., Watanabe H.;
RT "Cloning, sequencing and expression of the lexA-like gene of
RT Deinococcus radiodurans.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R1 / ATCC 13939 / DSM 20539 / NCIB 9279;
RX MEDLINE=20036896; PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus
RT radiodurans R1.";
RL Science 286:1571-1577(1999).

Feature:
CHAIN 1 210 LexA repressor.
/FTId=PRO_0000170030.
DNA_BIND 25 44 H-T-H motif.
ACT_SITE 120 120 Involved in auto-cleavage (By
similarity).
ACT_SITE 159 159 Involved in auto-cleavage (By
similarity).
SITE 84 85 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: 210

     MPPELTPTRR SILQATLRLG AGATAGQVAQ EVGITKQAIS QQVNILRKLG YLQPAETRYG
     PLQVTDRARA ALGEGLPIYG QIAAGIPALA EQSPEDFTPS IEALLGLKAG DFLLRVRGES
     MTGIGVMDGD YVVVRPAPEV HDGEVAVVLV PGDNAATLKR LYHFGQDILL TSENPAMPRL
     SFPAEQVQVQ GRMVGRVGVG APRVSHRVTE

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