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Description:
LexA repressor (EC 3.4.21.88).
Molecular weight: 23217
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:
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
07-MAR-2006, entry version 17.
Phylogenetic order:
Bacteria Proteobacteria Betaproteobacteria Burkholderiales Alcaligenaceae Bordetella.
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_BORPE:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | BX640416 | CAE42080.1 | - |
| MEROPS | S24.001 | -. | |
| GenomeReviews | BX470248_GR | BP1794.1 | |
| BioCyc | BPER520:BP1794-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 | IPR013324 | Sigma_r3_r4. | |
| 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=Tohama I / ATCC BAA-589 / NCTC 13251;
RX MEDLINE=22827954; PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
Feature:
CHAIN 1 216 LexA repressor.
/FTId=PRO_0000170016.
DNA_BIND 29 49 H-T-H motif (By similarity).
ACT_SITE 134 134 Involved in auto-cleavage (By
similarity).
ACT_SITE 171 171 Involved in auto-cleavage (By
similarity).
SITE 99 100 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: 216
MATKLTERQQ EILDLIRQTV ARTGFPPTRA EIAQALGFRS PNAAEDHLKA LARKGAIELT
AGASRGIRLK VPDSATPSAQ LTHPLLAQLV LPLVGRVAAG SPILASEHVE REVGVDPGLF
AQTPDYLLKV RGMSMRDAGI LEGDLLAVKR AAEARNGQIV VARLGDEVTV KRLQRQNGRI
ELLPENPDFA PIVVANTDEF ALEGIAVGLI RTQPLH