Q637D7 (LEXA_BACCZ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
LexA repressor
EC=3.4.21.88

Gene names

Name:	lexA
Ordered Locus Names:	BCE33L3395

Organism

Bacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP]

Taxonomic identifier

288681 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	206 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (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. HAMAP MF_00015
Catalytic activity	Hydrolysis of Ala-|-Gly bond in repressor lexA. HAMAP MF_00015
Subunit structure	Homodimer By similarity. HAMAP MF_00015
Sequence similarities	Belongs to the peptidase S24 family.
Sequence caution	The sequence AAU16868.1 differs from that shown. Reason: Erroneous initiation.

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: UniProtKB-KW DNA replication Inferred from electronic annotation. Source: UniProtKB-KW SOS response Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 206	206	LexA repressor HAMAP MF_00015		PRO_0000170005
Regions
	DNA binding	28 – 48	21	H-T-H motif By similarity
Sites
	Active site	128	1	For autocatalytic cleavage activity By similarity
	Active site	166	1	For autocatalytic cleavage activity By similarity
	Site	92 – 93	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q637D7 [UniParc]. Last modified February 1, 2005. Version 2. Checksum: CC4077E937DF8D09	FASTA	206	22,890
	10 20 30 40 50 60 MEKLTKRQQD ILDFIKLKVQ EKGYPPSVRE IGQAVGLASS STVHGHLSRL EEKGYIRRDP 70 80 90 100 110 120 TKPRAIEILG EDRMDTETQS VIQVPIVGKV TAGLPITAVE SVEEHFPLPA SIVAGADQVF 130 140 150 160 170 180 MLRISGDSMI EAGIFDGDLV VVRQQQSAYN GEIVVALTED NEATVKRFYK EKDHFRLQPE 190 200 NSSLEPIILK QVSVIGKVIG VYRDLH

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ZK / E33L.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000001 Genomic DNA. Translation: AAU16868.1. Different initiation.
RefSeq	YP_084980.1. NC_006274.1.
3D structure databases
ProteinModelPortal	Q637D7.
ModBase	Search...
Protein-protein interaction databases
STRING	Q637D7.
Protein family/group databases
MEROPS	S24.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000044379; EBBACP00000043280; EBBACG00000044370.
GeneID	3026916.
GenomeReviews	Gene locus BCE33L3395 in contig CP000001_GR.
KEGG	bcz:BCZK3395.
PATRIC	18890524. VBIBacCer95304_3600.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1974.
GeneTree	EBGT00050000002279.
HOGENOM	HBG679610.
PhylomeDB	Q637D7.
ProtClustDB	PRK00215.
Enzyme and pathway databases
BioCyc	BCER288681:BCE33L3395-MONOMER.
Family and domain databases
HAMAP	MF_00015. LexA. [Tree]
InterPro	IPR006199. LexA_DNA-bd_dom. IPR006200. Pept_S24_LexA. IPR006197. Peptidase_S24_LexA. IPR019759. Peptidase_S24_S26. IPR015927. Peptidase_S24_S26A/B/C. IPR011056. Peptidase_S24_S26A/B/C_b-rbn. IPR011991. WHTH_trsnscrt_rep_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.
KO	K01356.
Pfam	PF01726. LexA_DNA_bind. 1 hit. PF00717. Peptidase_S24. 1 hit. [Graphical view]
PRINTS	PR00726. LEXASERPTASE.
SUPFAM	SSF51306. Pept_S24_S26_C. 1 hit.
TIGRFAMs	TIGR00498. LexA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

LEXA_BACCZ

Accession

Primary (citable) accession number: Q637D7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	February 1, 2005
Last modified:	January 25, 2012
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program