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Description:
LexA repressor (EC 3.4.21.88).
Molecular weight: 26033
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-JUN-2002, sequence version 1.
07-MAR-2006, entry version 27.
Phylogenetic order:
Bacteria Proteobacteria Alphaproteobacteria Rhizobiales Rhizobiaceae Agrobacterium.
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_AGRT5:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AE009100 | AAL42401.1 | - |
| EMBL | AE008065 | AAK87187.1 | - |
| PIR | AC2748 | AC2748. | |
| PIR | B97529 | B97529. | |
| HSSP | P03033 | 1JHC | |
| GenomeReviews | AE007869_GR | AGR_C_2577.1 | |
| GenomeReviews | AE008688_GR | Atu1395.1 | |
| 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].
RX MEDLINE=21608550; PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P.,
RA Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L.,
RA Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr.,
RA Chapman P., Clendenning J., Deatherage G., Gillet W., Grant C.,
RA Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A.,
RA Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D.,
RA Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M.,
RA Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M.,
RA Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V.,
RA Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX MEDLINE=21608551; PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M.,
RA Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L.,
RA Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F.,
RA Wollam C., Allinger M., Doughty D., Scott C., Lappas C., Markelz B.,
RA Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G.,
RA Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
Feature:
CHAIN 1 240 LexA repressor.
/FTId=PRO_0000169998.
DNA_BIND 26 46 H-T-H motif (By similarity).
ACT_SITE 160 160 Involved in auto-cleavage (By
similarity).
ACT_SITE 198 198 Involved in auto-cleavage (By
similarity).
SITE 125 126 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: 240
MLTRKQQELL LFIHERMKES GVPPSFDEMK DALDLASKSG IHRLITALEE RGFIRRLPNR
ARALEVIKLP EAYTPGARPQ RGFSPSVIEG SLGKPKEPEP APAVKAPAND FAGAATIPVM
GRIAAGVPIS AIQNNTHDLA VPVDMLGSGE HYALEVKGDS MIEAGIFDGD TVIIRNGNTA
NPGDIVVALV DDEEATLKRF RRKGASIALE AANPAYETRI FGPDRVKIQG KLVGLIRRYH