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Description:
LexA repressor (EC 3.4.21.88).
Molecular weight: 22638
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:
25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
07-MAR-2006, entry version 26.
Phylogenetic order:
Bacteria Firmicutes Bacillales Listeriaceae Listeria.
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_LISMO:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AL591978 | CAC99380.1 | - |
| PIR | AF1237 | AF1237. | |
| HSSP | P03033 | 1JHF | |
| GenomeReviews | AL591824_GR | lmo1302.1 | |
| ListiList | LMO01302 | -.1 | |
| BioCyc | LMON169963:LMO1302-MONOMER | -.1 | |
| HAMAP | MF_00015 | - | 1. |
| InterPro | IPR006199 | LexA_DNA_bd. | |
| InterPro | IPR006200 | Pept_S24_LexA. | |
| InterPro | IPR006198 | Pept_S24_S26. | |
| InterPro | IPR006197 | Pept_S24_SOS. | |
| InterPro | IPR011991 | Wing_hlx_DNA_bd. | |
| Pfam | PF01726 | LexA_DNA_bind | 1. |
| Pfam | PF00717 | Peptidase_S24 | 1. |
| PRINTS | PR00726 | LEXASERPTASE. | |
| TIGRFAMs | TIGR00498 | lexA | 1. |
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=EGD-e / Serovar 1/2a;
RX MEDLINE=21537279; PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A.,
RA Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T.,
RA Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P.,
RA Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O.,
RA Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P.,
RA Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D.,
RA Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G.,
RA Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H.,
RA Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R.,
RA Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
Feature:
CHAIN 1 204 LexA repressor.
/FTId=PRO_0000170053.
DNA_BIND 27 47 H-T-H motif (By similarity).
ACT_SITE 126 126 Involved in auto-cleavage (By
similarity).
ACT_SITE 164 164 Involved in auto-cleavage (By
similarity).
SITE 90 91 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: 204
MKISKRQQDI YEFIKSEVKE KGYPPSVREI GEAVGLASSS TVHGHLARLE GKGLIRRDPT
KPRAIEILSL EDEAETPNVV NIPIIGKVTA GMPITAIENI DEYFPLPEYM AAGETNVFML
EIDGESMINA GILDGDKVIV RQESSAINGE IVVAMTDENE ATCKRFYKEA NHFRLQPEND
ALEPILLNNV TILGKVIGLY RDIR