ID LEXA_SALCH Reviewed; 202 AA.
AC Q57GZ0;
DT 02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 01-MAY-2013, entry version 60.
DE RecName: Full=LexA repressor;
DE EC=3.4.21.88;
GN Name=lexA; OrderedLocusNames=SCH_4116;
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67;
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y.,
RA Wang H.-S., Lee Y.-S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a
RT highly invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
CC -!- FUNCTION: Represses a number of genes involved in the response to
CC DNA damage (SOS response), including recA and lexA. Binds to the
CC 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence
CC of single-stranded DNA, RecA interacts with LexA causing an
CC 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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AE017220; AAX68022.1; -; Genomic_DNA.
DR RefSeq; YP_219103.1; NC_006905.1.
DR ProteinModelPortal; Q57GZ0; -.
DR SMR; Q57GZ0; 2-198.
DR STRING; 321314.SC4116; -.
DR MEROPS; S24.001; -.
DR PaxDb; Q57GZ0; -.
DR PRIDE; Q57GZ0; -.
DR EnsemblBacteria; AAX68022; AAX68022; SCH_4116.
DR GeneID; 3336662; -.
DR KEGG; sec:SC4116; -.
DR PATRIC; 32329647; VBISalEnt136302_4738.
DR eggNOG; COG1974; -.
DR KO; K01356; -.
DR OMA; RGDSMKN; -.
DR ProtClustDB; PRK00215; -.
DR BioCyc; SENT321314:GJCS-4312-MONOMER; -.
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-dependent; IEA:HAMAP.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0009432; P:SOS response; IEA:HAMAP.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.10.109.10; -; 1.
DR HAMAP; MF_00015; LexA; 1; -.
DR InterPro; IPR006199; LexA_DNA-bd_dom.
DR InterPro; IPR006200; Pept_S24_LexA.
DR InterPro; IPR006197; Peptidase_S24_LexA.
DR InterPro; IPR019759; Peptidase_S24_S26.
DR InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR InterPro; IPR011056; Peptidase_S24_S26A/B/C_b-rbn.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF01726; LexA_DNA_bind; 1.
DR Pfam; PF00717; Peptidase_S24; 1.
DR PRINTS; PR00726; LEXASERPTASE.
DR SUPFAM; SSF51306; Pept_S24_S26_C; 1.
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 1 202 LexA repressor.
FT /FTId=PRO_0000170080.
FT DNA_BIND 28 48 H-T-H motif (By similarity).
FT ACT_SITE 119 119 For autocatalytic cleavage activity (By
FT similarity).
FT ACT_SITE 156 156 For autocatalytic cleavage activity (By
FT similarity).
FT SITE 84 85 Cleavage; by autolysis (By similarity).
SQ SEQUENCE 202 AA; 22305 MW; 6BC34EA11A70430C CRC64;
MKALTARQQE VFDLIRDHIS QTGMPPTRAE IAQRLGFRSP NAAEEHLKAL ARKGVLEIVS
GASRGIRLLQ EEEDGLPLVG RVAAGEPLLA QQHIEGHYQV DPSLFKPSAD FLLRVSGMSM
KDIGIMDGDL LAVHKTQDVR NGQVVVARID DEVTVKRLKK QGNKVELLPE NSEFTPIVVD
LREQSFTIEG LAVGVIRNGE WL
//
