ID   LEXA_ANADE              Reviewed;         229 AA.
AC   Q2IIJ0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=LexA repressor;
DE            EC=3.4.21.88;
GN   Name=lexA; OrderedLocusNames=Adeh_1701;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000251; ABC81474.1; -; Genomic_DNA.
DR   RefSeq; YP_464911.1; -.
DR   GeneID; 3887649; -.
DR   GenomeReviews; CP000251_GR; Adeh_1701.
DR   KEGG; ade:Adeh_1701; -.
DR   HOGENOM; Q2IIJ0; -.
DR   OMA; Q2IIJ0; KVIGVFR.
DR   BioCyc; ADEH290397:ADEH_1701-MON; -.
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    229       LexA repressor.
FT                                /FTId=PRO_1000001255.
FT   DNA_BIND     28     48       H-T-H motif (By similarity).
FT   ACT_SITE    147    147       For autocatalytic cleavage activity (By
FT                                similarity).
FT   ACT_SITE    184    184       For autocatalytic cleavage activity (By
FT                                similarity).
FT   SITE        111    112       Cleavage; by autolysis (By similarity).
SQ   SEQUENCE   229 AA;  25071 MW;  CEC54734F74E898F CRC64;
     MEGLTDRQLE VLRFIASQIE DHGYPPTIRE IGEALDIRST NGVNDHLKAL ERKGYLSRDP
     VKSRALIPTS AAREALGGGG EAGSNVVPLV RGPARPGSRM IEIPIVGRVA AGMPILAQER
     VEDTVQVDAF LLGTNKKVYG LRVQGDSMIG DGILPGDYVF VKKQLNADDG EIVVAMIDDE
     ATVKRVYFEG DRVRFQPSNP RMAPIYVRHS DFRSTMILGV VVGVYRKLT
//