Reviewed, UniProtKB/Swiss-Prot P31080 (LEXA_BACSU)

Names and origin

Protein names

Recommended name:
    LexA repressor
    EC=3.4.21.88
Alternative name(s):
    SOS regulatory protein dinR

Gene names

Name:	lexA
Synonyms:	dinR
Ordered Locus Names:	BSU17850

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	205 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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. HAMAP MF_00015
Catalytic activity	Hydrolysis of Ala-|-Gly bond in repressor lexA. HAMAP MF_00015
Subunit structure	Homodimer By similarity.
Developmental stage	Expressed during the entire cell cycle with at least a threefold increase when cells develop competence. HAMAP MF_00015
Induction	An SOS-independent induction of dinR occurs during competence. HAMAP MF_00015
Sequence similarities	Belongs to the peptidase S24 family.

Ontologies

Keywords
Biological process	DNA damage DNA repair DNA replication SOS response Transcription Transcription regulation
Ligand	DNA-binding
Molecular function	Hydrolase Repressor
PTM	Autocatalytic cleavage
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: HAMAP DNA replication Inferred from electronic annotation. Source: HAMAP SOS response Inferred from electronic annotation. Source: HAMAP negative regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: HAMAP proteolysis Inferred from electronic annotation. Source: InterPro transcription Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	DNA binding Inferred from electronic annotation. Source: HAMAP serine-type endopeptidase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 205	205	LexA repressor HAMAP MF_00015		PRO_0000170010
Regions
	DNA binding	28 – 48	21	H-T-H motif By similarity
Sites
	Active site	127	1	For autocatalytic cleavage activity By similarity
	Active site	165	1	For autocatalytic cleavage activity By similarity
	Site	91 – 92	2	Cleavage; by autolysis HAMAP MF_00015

Sequences

	Sequence		Length	Mass (Da)
	P31080-1 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 68EA3EC2FD950B1B	FASTA	205	22,849
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of dinR, a DNA damage-inducible regulator gene of Bacillus subtilis." Raymond-Denise A., Guillen N. J. Bacteriol. 173:7084-7091(1991) [PubMed: 1657879] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The Bacillus subtilis dinR gene codes for the analogue of Escherichia coli LexA. Purification and characterization of the DinR protein." Miller M.C., Resnick J.B., Smith B.T., Lovett C.M. Jr. J. Biol. Chem. 271:33502-33508(1996) [PubMed: 8969214] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: 168 / YB886.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." 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. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"The Bacillus subtilis DinR binding site: redefinition of the consensus sequence." Winterling K.W., Chafin D., Hayes J.J., Sun J., Levine A.S., Yasbin R.E., Woodgate R. J. Bacteriol. 180:2201-2211(1998) [PubMed: 9555905] [Abstract] Cited for: DNA-BINDING SPECIFICITY, POSSIBLE DIMERIZATION. Strain: YB886A.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M64684 Genomic DNA. Translation: AAA22573.1. AL009126 Genomic DNA. Translation: CAB13669.1.
PIR	A41315.
RefSeq	NP_389668.1.
3D structure databases
HSSP	HSSP built from PDB template 1JHF based on UniProtKB P03033.
ModBase	Search...
Protein family/group databases
MEROPS	S24.001.
Genome annotation databases
GeneID	939564.
GenomeReviews	Gene locus BSU17850 in contig AL009126_GR.
KEGG	bsu:BSU17850.
NMPDR	fig|224308.1.peg.1789.
Organism-specific databases
SubtiList	BG10678. lexA. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P31080.
OMA	P31080. KVIGVFR.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU1786-MON.
BRENDA	3.4.21.88. 150.
Family and domain databases
HAMAP	MF_00015. [Tree]
InterPro	IPR006199. LexA_DNA_bd. IPR006200. Pept_S24_LexA. IPR006197. Peptidase_S24_LexA_cons-reg. IPR019759. Peptidase_S24_S26_cons-reg. IPR011056. Peptidase_S24_S26A/B/C_b-rbn. IPR011991. Wing_hlx_DNA_bd. [Graphical view]
Gene3D	G3DSA:2.10.109.10. Pept_S24_S26_C. 1 hit. G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
Pfam	PF01726. LexA_DNA_bind. 1 hit. PF00717. Peptidase_S24. 1 hit. [Graphical view]
PRINTS	PR00726. LEXASERPTASE.
TIGRFAMs	TIGR00498. lexA. 1 hit.
ProtoNet	Search...
Other Resources
PMAP-CutDB	P31080.

Entry information

Entry name

LEXA_BACSU

Accession

Primary (citable) accession number: P31080

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	June 16, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)