Q7VRY0 (LEXA_BORPE) 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:	BP1794

Organism

Bordetella pertussis

Taxonomic identifier

520 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	216 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.

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 Reference 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 – 216	216	LexA repressor HAMAP MF_00015		PRO_0000170016
Regions
	DNA binding	29 – 49	21	H-T-H motif By similarity
Sites
	Active site	134	1	For autocatalytic cleavage activity By similarity
	Active site	171	1	For autocatalytic cleavage activity By similarity
	Site	99 – 100	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7VRY0 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 9E3DB151FA064A72	FASTA	216	23,217
	10 20 30 40 50 60 MATKLTERQQ EILDLIRQTV ARTGFPPTRA EIAQALGFRS PNAAEDHLKA LARKGAIELT 70 80 90 100 110 120 AGASRGIRLK VPDSATPSAQ LTHPLLAQLV LPLVGRVAAG SPILASEHVE REVGVDPGLF 130 140 150 160 170 180 AQTPDYLLKV RGMSMRDAGI LEGDLLAVKR AAEARNGQIV VARLGDEVTV KRLQRQNGRI 190 200 210 ELLPENPDFA PIVVANTDEF ALEGIAVGLI RTQPLH

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tohama I / ATCC BAA-589 / NCTC 13251.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640416 Genomic DNA. Translation: CAE42080.1.
RefSeq	NP_880500.1. NC_002929.2.
3D structure databases
ProteinModelPortal	Q7VRY0.
SMR	Q7VRY0. Positions 5-69, 91-213.
ModBase	Search...
Protein family/group databases
MEROPS	S24.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2667248.
GenomeReviews	Gene locus BP1794 in contig BX470248_GR.
KEGG	bpe:BP1794.
PATRIC	21156866. VBIBorPer7866_1926.
Phylogenomic databases
HOGENOM	HBG679610.
OMA	IAENPDF.
PhylomeDB	Q7VRY0.
ProtClustDB	PRK00215.
Enzyme and pathway databases
BioCyc	BPER257313:BP1794-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_BORPE

Accession

Primary (citable) accession number: Q7VRY0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2004
Last sequence update:	October 1, 2003
Last modified:	January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program