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Description:
LexA repressor (EC 3.4.21.88).
Molecular weight: 22358
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:
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
07-MAR-2006, entry version 13.
Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Enterobacteriales Enterobacteriaceae Escherichia.
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_ECOLI:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | J01643 | AAA24067.1 | - |
| EMBL | U00006 | AAC43137.1 | - |
| EMBL | U00096 | AAC77013.1 | - |
| EMBL | L02362 | AAA24068.1 | - |
| PIR | A90808 | ILEC. | |
| PDB | 1JHC | X-ray | A=68-202. |
| PDB | 1JHE | X-ray | A/B=68-202. |
| PDB | 1JHF | X-ray | A/B=1-202. |
| PDB | 1JHH | X-ray | A/B=1-202. |
| PDB | 1LEA | NMR | @=1-84. |
| PDB | 1LEB | NMR | @=1-84. |
| PDB | 1MVD | Model | A/B=1-202. |
| PDB | 1QAA | Model | A/B=1-202. |
| MEROPS | S24.001 | -. | |
| GenomeReviews | U00096_GR | b4043.1 | |
| EchoBASE | EB0528 | -.1 | |
| EcoGene | EG10533 | lexA. | |
| LinkHub | P0A7C2 | -.1 | |
| GO | GO:0005515 | F:protein binding | IPI. |
| HAMAP | MF_00015 | - | 1. |
| InterPro | IPR006200 | Pept_S24_LexA. | |
| 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:
3D-structure; 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].
RX MEDLINE=81186269; PubMed=7013987; DOI=10.1016/0092-8674(81)90432-3;
RA Horii T., Ogawa T., Ogawa H.;
RT "Nucleotide sequence of the lexA gene of E. coli.";
RL Cell 23:689-697(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANT LEXA3.
RC STRAIN=K12;
RX MEDLINE=82059453; PubMed=6272195;
RA Markham B.E., Little J.W., Mount D.W.;
RT "Nucleotide sequence of the lexA gene of Escherichia coli K-12.";
RL Nucleic Acids Res. 9:4149-4161(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MG1655;
RX MEDLINE=94089392; PubMed=8265357;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J.,
RA Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the
RT region from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655;
RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-93.
RX MEDLINE=91080864; PubMed=2259342; DOI=10.1007/BF00315795;
RA Oertel-Buchheit P., Lamerichs R.M., Schnarr M., Granger-Schnarr M.;
RT "Genetic analysis of the LexA repressor: isolation and
RT characterization of LexA(Def) mutant proteins.";
RL Mol. Gen. Genet. 223:40-48(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RX MEDLINE=81174720; PubMed=6261224;
RA Miki T., Ebina Y., Kishi F., Nakazawa A.;
RT "Organization of the lexA gene of Escherichia coli and nucleotide
RT sequence of the regulatory region.";
RL Nucleic Acids Res. 9:529-543(1981).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 195-202.
RC STRAIN=K12;
RA Lilley P.E., Dixon N.E.;
RL Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION.
RX MEDLINE=82037806; PubMed=7027255;
RA Little J.W., Mount D.W., Yanisch-Perron C.R.;
RT "Purified lexA protein is a repressor of the recA and lexA genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:4199-4203(1981).
RN [9]
RP FUNCTION.
RX MEDLINE=82037807; PubMed=7027256;
RA Brent R., Ptashne M.;
RT "Mechanism of action of the lexA gene product.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:4204-4208(1981).
RN [10]
RP STRUCTURE BY NMR.
RX MEDLINE=89386639; PubMed=2780544;
RA Lamerichs R.M.J.N., Padilla A., Boelens R., Kaptein R., Ottleben G.,
RA Rueterjans H., Granger-Schnarr M., Oertel P., Schnarr M.;
RT "The amino-terminal domain of LexA repressor is alpha-helical but
RT differs from canonical helix-turn-helix proteins: a two-dimensional 1H
RT NMR study.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:6863-6867(1989).
RN [11]
RP STRUCTURE BY NMR.
RX MEDLINE=94357165; PubMed=8076591;
RA Fogh R.H., Ottleben G., Rueterjans H., Schnarr M., Boelens R.,
RA Kaptein R.;
RT "Solution structure of the LexA repressor DNA binding domain
RT determined by 1H NMR spectroscopy.";
RL EMBO J. 13:3936-3944(1994).
RN [12]
RP 3D-STRUCTURE MODELING.
RX MEDLINE=95303877; PubMed=7784426; DOI=10.1002/prot.340210305;
RA Knegtel R.M.A., Fogh R.H., Ottleben G., Rueterjans H., Dumoulin P.,
RA Schnarr M., Boelens R., Kaptein R.;
RT "A model for the LexA repressor DNA complex.";
RL Proteins 21:226-236(1995).
Feature:
CHAIN 1 202 LexA repressor.
/FTId=PRO_0000170031.
DNA_BIND 28 48 H-T-H motif.
ACT_SITE 119 119 Involved in auto-cleavage (By
similarity).
ACT_SITE 156 156 Involved in auto-cleavage (By
similarity).
SITE 84 85 Cleavage (auto-).
VARIANT 85 85 G -> D (in lexA3, resistant to cleavage).
STRAND 96 98
STRAND 100 100
HELIX 102 104
STRAND 111 114
TURN 119 120
HELIX 121 123
TURN 124 124
TURN 127 128
STRAND 130 135
TURN 141 142
STRAND 144 149
STRAND 153 161
TURN 162 163
STRAND 164 168
TURN 172 173
STRAND 177 180
TURN 181 183
STRAND 186 197
Comments:
-!- FUNCTION: Represses a number of genes involved in the response to
DNA damage (SOS response), including recA and lexA. Binds to the
16 bp palindromic sequence 5'-CTGTATATATATACAG-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.
-!- INTERACTION:
P0A7W1:rpsE; NbExp=1; IntAct=EBI-553416, EBI-543949;
-!- SIMILARITY: Belongs to the peptidase S24 family.
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Sequence length: 202
MKALTARQQE VFDLIRDHIS QTGMPPTRAE IAQRLGFRSP NAAEEHLKAL ARKGVIEIVS
GASRGIRLLQ EEEEGLPLVG RVAAGEPLLA QQHIEGHYQV DPSLFKPNAD FLLRVSGMSM
KDIGIMDGDL LAVHKTQDVR NGQVVVARID DEVTVKRLKK QGNKVELLPE NSEFKPIVVD
LRQQSFTIEG LAVGVIRNGD WL