Q8P9X2 (LEXA2_XANCP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
LexA repressor 2
EC=3.4.21.88

Gene names

Name:	lexA2
Ordered Locus Names:	XCC1721

Organism

Xanthomonas campestris pv. campestris

Taxonomic identifier

340 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas

Protein attributes

Sequence length	213 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 – 213	213	LexA repressor 2 HAMAP MF_00015		PRO_0000170110
Regions
	DNA binding	27 – 47	21	H-T-H motif By similarity
Sites
	Active site	133	1	For autocatalytic cleavage activity By similarity
	Active site	170	1	For autocatalytic cleavage activity By similarity
	Site	98 – 99	2	Cleavage; by autolysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8P9X2 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: C43E270DA737A106	FASTA	213	23,149
	10 20 30 40 50 60 MGLTDTQQAI LALIAERIET DGVPPSQTEI ARAFGFKGVR AAQYHLEALE QAGAIRRVPG 70 80 90 100 110 120 QARGIRLAGA AAHARAAPAE EPVRDDVLRL PVLGRVAAGL PIGADIGSDD FVVLDRVFFS 130 140 150 160 170 180 PSPDYLLKVQ GDSMRDEGIF NGDLIGVHRT RDARSGQIVV ARIDEEITVK LLKIGKDRIR 190 200 210 LLPRNPDYAP IEVLPDQDFA IEGLYCGLLR PNR

References

[1]

"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities." da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P. Nature 417:459-463(2002) [PubMed: 12024217] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33913 / NCPPB 528 / LMG 568.

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Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008922 Genomic DNA. Translation: AAM41015.1.
RefSeq	NP_637091.1. NC_003902.1.
3D structure databases
ProteinModelPortal	Q8P9X2.
ModBase	Search...
Protein family/group databases
MEROPS	S24.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	998323.
GenomeReviews	Gene locus XCC1721 in contig AE008922_GR.
KEGG	xcc:XCC1721.
PATRIC	24074247. VBIXanCam115730_1837.
Phylogenomic databases
HOGENOM	HBG679610.
OMA	THRHSPS.
ProtClustDB	PRK00215.
Enzyme and pathway databases
BioCyc	XCAM190485:XCC1721-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

LEXA2_XANCP

Accession

Primary (citable) accession number: Q8P9X2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2002
Last sequence update:	October 1, 2002
Last modified:	January 25, 2012
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program