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UniProtKB/Swiss-Prot entry P31080


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LEXA_BACSU
Primary accession number P31080
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on July 1, 1993 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 73)
Name and origin of the protein
Protein name LexA repressor
Synonyms EC 3.4.21.88
SOS regulatory protein dinR
Gene name
Name: lexA
Synonyms: dinR
OrderedLocusNames: BSU17850
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=1657879 [NCBI, ExPASy, EBI, Israel, Japan]
Raymond-Denise A., Guillen N.;
"Identification of dinR, a DNA damage-inducible regulator gene of Bacillus subtilis.";
J. Bacteriol. 173:7084-7091(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
STRAIN=168 / YB886;
DOI=10.1074/jbc.271.52.33176; PubMed=8969214 [NCBI, ExPASy, EBI, Israel, Japan]
Miller M.C., Resnick J.B., Smith B.T., Lovett C.M. Jr.;
"The Bacillus subtilis dinR gene codes for the analogue of Escherichia coli LexA. Purification and characterization of the DinR protein.";
J. Biol. Chem. 271:33502-33508(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[4]
DNA-BINDING SPECIFICITY, AND POSSIBLE DIMERIZATION.
STRAIN=YB886A;
PubMed=9555905 [NCBI, ExPASy, EBI, Israel, Japan]
Winterling K.W., Chafin D., Hayes J.J., Sun J., Levine A.S., Yasbin R.E., Woodgate R.;
"The Bacillus subtilis DinR binding site: redefinition of the consensus sequence.";
J. Bacteriol. 180:2201-2211(1998).
Comments
  • FUNCTION: Represses dinA, dinB, dinC, recA genes and itself by binding 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).
  • DEVELOPMENTAL STAGE: Expressed during the entire cell cycle with at least a threefold increase when cells develop competence.
  • INDUCTION: An SOS-independent induction of dinR occurs during competence.
  • SIMILARITY: Belongs to the peptidase S24 family [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M64684; AAA22573.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99113; CAB13669.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A41315; A41315.
RefSeq NP_389668.1; -.
3D structure databases
HSSP P03033; 1JHF. [HSSP ENTRY / PDB]
ModBase P31080.
Protein family/group databases
MEROPS S24.001; -.
Enzyme and pathway databases
BioCyc BSUB224308:BSU1786-MON; -.
Organism-specific databases
SubtiList BG10678; lexA. [Micado]
Ontologies
GO
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from HAMAP).
GO:0004252; Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from HAMAP).
GO:0006281; Biological process: DNA repair (inferred from electronic annotation from HAMAP).
GO:0006260; Biological process: DNA replication (inferred from electronic annotation from HAMAP).
GO:0045892; Biological process: negative regulation of transcription, DNA-dependent (inferred from electronic annotation from HAMAP).
GO:0006508; Biological process: proteolysis (inferred from electronic annotation from InterPro).
GO:0009432; Biological process: SOS response (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00015; -; 1.
PBIL [Tree]
InterPro IPR006199; LexA_DNA_bd.
IPR006200; Pept_S24_LexA.
IPR006197; Pept_S24_SOS.
IPR011056; Peptidase_S24_S26_C.
IPR011991; Wing_hlx_DNA_bd.
Graphical view of domain structure.
Gene3D G3DSA:2.10.109.10; Pept_S24_S26_C; 1.
G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
Pfam PF01726; LexA_DNA_bind; 1.
PF00717; Peptidase_S24; 1.
Pfam graphical view of domain structure.
PRINTS PR00726; LEXASERPTASE.
TIGRFAMs TIGR00498; lexA; 1.
BLOCKS P31080.
ProtoNet P31080.
Genome annotation databases
GeneID 939564; -.
GenomeReviews AL009126_GR; BSU17850.
KEGG bsu:BSU17850; -.
NMPDR fig|224308.1.peg.1789; -.
Phylogenomic databases
HOGENOM P31080; -.
Genome annotation databases
CMR P31080; BSU17850.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Autocatalytic cleavage; Complete proteome; DNA damage; DNA repair; DNA replication; DNA-binding; Hydrolase; Repressor; SOS response; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   205  205     LexA repressor. PRO_0000170010
DNA_BIND   28    48  21     H-T-H motif (By similarity). 
ACT_SITE   127   127        For autocatalytic cleavage activity (By similarity). 
ACT_SITE   165   165        For autocatalytic cleavage activity (By similarity). 
SITE   91    92  2     Cleavage; by autolysis. 
Sequence information
Length: 205 AA [This is the length of the unprocessed precursor] Molecular weight: 22849 Da [This is the MW of the unprocessed precursor] CRC64: 68EA3EC2FD950B1B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTKLSKRQLD ILRFIKAEVK SKGYPPSVRE IGEAVGLASS STVHGHLARL ETKGLIRRDP 

        70         80         90        100        110        120 
TKPRAIEILD EEVDIPQSQV VNVPVIGKVT AGSPITAVEN IEEYFPLPDR MVPPDEHVFM 

       130        140        150        160        170        180 
LEIMGDSMID AGILDKDYVI VKQQNTANNG EIVVAMTEDD EATVKRFYKE DTHIRLQPEN 

       190        200 
PTMEPIILQN VSILGKVIGV FRTVH 

P31080 in FASTA format

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