[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.; "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16."; Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.

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 [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

AP006627; BAD64702.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_175663.1; -.

3D structure databases

ModBase

Q5WG03.

Enzyme and pathway databases

BioCyc

BCLA66692:ABC2167-MON; -.

Ontologies

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: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.

TIGR00498; lexA; 1.

Genome annotation databases

GeneID

3204066; -.

GenomeReviews

AP006627_GR; ABC2167.

KEGG

bcl:ABC2167; -.

NMPDR

fig|66692.3.peg.2471; -.

Phylogenomic databases

HOGENOM

Q5WG03; -.

Genome annotation databases

CMR

Q5WG03; ABC2167.

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

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 208`	`208`	`LexA repressor.`	`PRO_0000170009`
`DNA_BIND`	`28 48`	`21`	`H-T-H motif (By similarity).`
`ACT_SITE`	`130 130`		`For autocatalytic cleavage activity (By similarity).`
`ACT_SITE`	`168 168`		`For autocatalytic cleavage activity (By similarity).`
`SITE`	`95 96`	`2`	`Cleavage; by autolysis (By similarity).`

Sequence information

Length: 208 AA [This is the length of the unprocessed precursor]

Molecular weight: 23179 Da [This is the MW of the unprocessed precursor]

CRC64: 4C967CAB4A10F24B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSKLSKRQEE ILAYIKDEVK KKGYPPSVRE IGEAVGLASS STVHGHLARL EKKGYIRRDP 

        70         80         90        100        110        120 
TKPRAIEVLS LGFDNDTFVK KETASFIPVI GKVTAGVPIT AVENVEDYLP LPDHLAAYDN 

       130        140        150        160        170        180 
TYALVIQGES MIEAGIYDGD QVIVRQQQTA DNGDIIVAMT EDNEATVKRF FREKDYIRLQ 

       190        200 
PENSSMEPII LENCTILGKV IGVFRTIH

Q5WG03 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools