Description:
LexA repressor (EC 3.4.21.88).
Molecular weight: 23095
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:
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
07-MAR-2006, entry version 52.
Phylogenetic order:
Bacteria Actinobacteria Actinobacteridae Actinomycetales Corynebacterineae Mycobacteriaceae Mycobacterium Mycobacterium tuberculosis complex.
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_MYCTU:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | X91407 | CAA62750.1 | - |
| EMBL | BX842580 | CAB09461.1 | - |
| EMBL | AE000516 | AAK47109.1 | - |
| PIR | C70533 | C70533. | |
| HSSP | P03033 | 1JHC | |
| GenomeReviews | AE000516_GR | MT2793.1 | |
| GenomeReviews | AL123456_GR | Rv2720.1 | |
| TIGR | MT2793 | -. | |
| TubercuList | Rv2720 | -. | |
| 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 [GENOMIC DNA], AND DNA-BINDING SPECIFICITY.
RC STRAIN=H37Rv;
RX MEDLINE=97237722; PubMed=9084177;
RA Movahedzadeh F., Colston M.J., Davis E.O.;
RT "Characterization of Mycobacterium tuberculosis LexA: recognition of a
RT Cheo (Bacillus-type SOS) box.";
RL Microbiology 143:929-936(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H37Rv;
RX MEDLINE=98295987; PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M.,
RA Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the
RT complete genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX MEDLINE=22206494; PubMed=12218036;
RX DOI=10.1128/JB.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H.,
RA Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D.,
RA Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M.,
RA Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C.,
RA Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
Feature:
CHAIN 1 217 LexA repressor.
/FTId=PRO_0000170059.
DNA_BIND 32 52 H-T-H motif (By similarity).
ACT_SITE 141 141 Involved in auto-cleavage (By
similarity).
ACT_SITE 178 178 Involved in auto-cleavage (By
similarity).
SITE 106 107 Cleavage (auto-) (By similarity).
Comments:
-!- FUNCTION: Represses a number of genes involved in the response to
DNA damage (SOS response), including recA and lexA. Has been shown
to bind to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'. 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.
-!- 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: 217
MLSADSALTE RQRTILDVIR ASVTSRGYPP SIREIGDAVG LTSTSSVAHQ LRTLERKGYL
RRDPNRPRAV NVRGADDAAL PPVTEVAGSD ALPEPTFVPV LGRIAAGGPI LAEEAVEDVF
PLPRELVGEG TLFLLKVIGD SMVEAAICDG DWVVVRQQNV ADNGDIVAAM IDGEATVKTF
KRAGGQVWLM PHNPAFDPIP GNDATVLGKV VTVIRKV