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Description:
LexA repressor (EC 3.4.21.88).
Molecular weight: 22619
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:
28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
28-MAR-2003, sequence version 2.
07-MAR-2006, entry version 23.
Phylogenetic order:
Bacteria Spirochaetes Spirochaetales Leptospiraceae Leptospira.
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_LEPIN:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AE011325 | AAN48646.1 | ALT_INIT |
| HSSP | P03033 | 1JHC | |
| GenomeReviews | AE010300_GR | LA1447.1 | |
| BioCyc | LINT189518:LA1447-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=56601 / Serogroup Icterohaemorrhagiae / Serovar lai;
RX MEDLINE=22598143; PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H.,
RA Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F.,
RA Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F.,
RA Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W.,
RA Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A.,
RA Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z.,
RA Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira
RT interrogans revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
Feature:
CHAIN 1 203 LexA repressor.
/FTId=PRO_0000170050.
DNA_BIND 28 47 H-T-H motif (By similarity).
ACT_SITE 127 127 Involved in auto-cleavage (By
similarity).
ACT_SITE 164 164 Involved in auto-cleavage (By
similarity).
SITE 91 92 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: 203
MKDLTDKQQA VLAFITAIIK ERGFPPTIRE IGDEFGITAK GAYDHLKAIE KKGYLKTAKN
QSRAIELIRQ SPMESLPVQA TSIPVIGQVA AGLPIFAEEN IESYIPVPDE MAKGNVPMYA
LRVQGDSMIE VGINDGDIAI IEKRDIARNG EIVVALIEDE ATLKVYYKEQ DQIRLEARNP
KYKPIKTKKA TVMGKLIGLY RIY