ID   LEXA_BARHE              Reviewed;         234 AA.
AC   Q6G5D9;
DT   02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 32.
DE   RecName: Full=LexA repressor;
DE            EC=3.4.21.88;
GN   Name=lexA; OrderedLocusNames=BH08420;
OS   Bartonella henselae (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=38323;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / Houston 1;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic
RT   derivative of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
CC   -!- FUNCTION: Represses a number of genes involved in the response to
CC       DNA damage (SOS response), including recA and lexA. In the
CC       presence of single-stranded DNA, recA interacts with lexA causing
CC       an autocatalytic cleavage which disrupts the DNA-binding part of
CC       lexA, leading to derepression of the SOS regulon and eventually
CC       DNA repair (By similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of Ala-|-Gly bond in repressor
CC       lexA.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase S24 family.
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DR   EMBL; BX897699; CAF27641.1; -; Genomic_DNA.
DR   RefSeq; YP_033648.1; -.
DR   MEROPS; S24.001; -.
DR   GeneID; 2865581; -.
DR   GenomeReviews; BX897699_GR; BH08420.
DR   KEGG; bhe:BH08420; -.
DR   NMPDR; fig|283166.1.peg.776; -.
DR   HOGENOM; Q6G5D9; -.
DR   OMA; Q6G5D9; HRSNEAR.
DR   BioCyc; BHEN283166:BH08420-MON; -.
DR   BRENDA; 3.4.21.88; 277357.
DR   GO; GO:0003677; F:DNA binding; IEA:HAMAP.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:HAMAP.
DR   GO; GO:0006281; P:DNA repair; IEA:HAMAP.
DR   GO; GO:0006260; P:DNA replication; IEA:HAMAP.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-d...; IEA:HAMAP.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0009432; P:SOS response; IEA:HAMAP.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   HAMAP; MF_00015; -; 1.
DR   InterPro; IPR006199; LexA_DNA_bd.
DR   InterPro; IPR006200; Pept_S24_LexA.
DR   InterPro; IPR006197; Peptidase_S24_LexA_cons-reg.
DR   InterPro; IPR019759; Peptidase_S24_S26_cons-reg.
DR   InterPro; IPR011056; Peptidase_S24_S26A/B/C_b-rbn.
DR   InterPro; IPR011991; Wing_hlx_DNA_bd.
DR   Gene3D; G3DSA:2.10.109.10; Pept_S24_S26_C; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF01726; LexA_DNA_bind; 1.
DR   Pfam; PF00717; Peptidase_S24; 1.
DR   PRINTS; PR00726; LEXASERPTASE.
DR   TIGRFAMs; TIGR00498; lexA; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; Complete proteome; DNA damage; DNA repair;
KW   DNA replication; DNA-binding; Hydrolase; Repressor; SOS response;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    234       LexA repressor.
FT                                /FTId=PRO_0000170011.
FT   DNA_BIND     26     46       H-T-H motif (By similarity).
FT   ACT_SITE    155    155       For autocatalytic cleavage activity (By
FT                                similarity).
FT   ACT_SITE    193    193       For autocatalytic cleavage activity (By
FT                                similarity).
SQ   SEQUENCE   234 AA;  26776 MW;  5636366052126E51 CRC64;
     MLTCKQYELL LFIHNHMKET GVPPSFDEMK TALELTSKSG IHRLITALEE RGFIRRLPNR
     ARAVEVIRLP EKITFNLSSA RKISPSVIEN NKRKISKNSD NFDLEEKKNI IIPIMGRIAA
     AVPISAIQQQ INTLCLPQDM ISLGEHYALE VKDDSMIEAG ILDKDIIIVR RQNTATSGEI
     IIALIDKEEV TFKRYRRKGN SITLEAANPH YETRIYRPER VQIQGKLIGL IRKY
//