ID   LEXA_AERHH              Reviewed;         207 AA.
AC   Q44069; A0KEQ1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 2.
DT   16-JUN-2009, entry version 59.
DE   RecName: Full=LexA repressor;
DE            EC=3.4.21.88;
GN   Name=lexA; OrderedLocusNames=AHA_0183;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95172406; PubMed=7867953; DOI=10.1016/0378-1119(94)00836-H;
RA   Riera J., Barbe J.;
RT   "Cloning, sequence and regulation of expression of the lexA gene of
RT   Aeromonas hydrophila.";
RL   Gene 154:71-75(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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; X77263; CAA54479.1; -; Genomic_DNA.
DR   EMBL; CP000462; ABK36241.1; -; Genomic_DNA.
DR   PIR; JC4042; JC4042.
DR   RefSeq; YP_854716.1; -.
DR   HSSP; P03033; 1JHH.
DR   SMR; Q44069; 2-203.
DR   MEROPS; S24.001; -.
DR   GeneID; 4486813; -.
DR   GenomeReviews; CP000462_GR; AHA_0183.
DR   KEGG; aha:AHA_0183; -.
DR   TIGR; AHA_0183; -.
DR   OMA; Q44069; KVIGVFR.
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    207       LexA repressor.
FT                                /FTId=PRO_0000169997.
FT   DNA_BIND     28     48       H-T-H motif (By similarity).
FT   ACT_SITE    124    124       For autocatalytic cleavage activity (By
FT                                similarity).
FT   ACT_SITE    161    161       For autocatalytic cleavage activity (By
FT                                similarity).
FT   SITE         89     90       Cleavage; by autolysis (By similarity).
FT   CONFLICT     92     92       P -> S (in Ref. 1; CAA54479).
SQ   SEQUENCE   207 AA;  22908 MW;  A5C4891A9196B960 CRC64;
     MKPLTPRQAE VLELIKANMN ETGMPPTRAE IAQKLGFKSA NAAEEHLKAL AKKGVIEIMP
     GTSRGIRLLL EEEEPLEESG LPLIGKVAAG EPILAQEHIE SHYQVDPALF HPRADFLLRV
     QGMSMKNIGI LDGDLLAVHK TQEVRNGQVV VARLDEDVTV KRFQRKGSQV WLLPENEELS
     PIEVDLSCQQ LTIEGLAVGV IRNADWM
//