NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=T / IAM 14863;
DOI=10.1093/nar/gkh830; PubMed=15383646 [NCBI, ExPASy, EBI, Israel, Japan]
Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K., Ikeda H., Hattori M., Beppu T.;
"Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium that depends on microbial commensalism.";
Nucleic Acids Res. 32:4937-4944(2004).

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

AP006840; BAD40721.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_075565.1; -.

3D structure databases

ModBase

Q67NM2.

Enzyme and pathway databases

BioCyc

STHE292459:STH1736-MON; -.

BRENDA

3.4.21.88; 20615.

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:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
GO:0009432;	Biological process: SOS response (inferred from electronic annotation from HAMAP).
GO:0006350;	Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_00015; -; 1.
PBIL [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 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.

Genome annotation databases

GeneID

2979854; -.

GenomeReviews

AP006840_GR; STH1736.

KEGG

sth:STH1736; -.

NMPDR

fig|292459.1.peg.1674; -.

Phylogenomic databases

HOGENOM

Q67NM2; -.

OMA

Q67NM2; KVIGVFR.

Genome annotation databases

CMR

Q67NM2; STH1736.

Other

ProtoNet

Q67NM2.

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`	`1 205`	`205`	`LexA repressor.`	`PRO_0000170097`
`DNA_BIND`	`29 49`	`21`	`H-T-H motif (By similarity).`
`ACT_SITE`	`128 128`		`For autocatalytic cleavage activity (By similarity).`
`ACT_SITE`	`165 165`		`For autocatalytic cleavage activity (By similarity).`
`SITE`	`91 92`	`2`	`Cleavage; by autolysis (By similarity).`

Sequence information

Length: 205 AA [This is the length of the unprocessed precursor]

Molecular weight: 23097 Da [This is the MW of the unprocessed precursor]

CRC64: 8CAD209C0B362258 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPEPLTERQR QILQFIKDEI RTKGYPPSVR EIGEAIGLSS SSTVHGHMTR LEEKGYIRRD 

        70         80         90        100        110        120 
PTKPRAIEVL DGSHTQLKRT IAVPVVGRVT AGQPILAQES IEDHFPLPAD FVRADESELF 

       130        140        150        160        170        180 
FLTVQGDSMI EAGILDGDYV LVHRQQHANN GDIVVALIED EATVKRFFKE QDHIRLQPEN 

       190        200 
RFMDPIIVPD CQILGKVVGL VRRMG

Q67NM2 in FASTA format

View entry in raw text format (no links)
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	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