GenomeNet

Database: UniProt/SWISS-PROT
Entry: LEXA_SALCH
LinkDB: LEXA_SALCH
Original site: LEXA_SALCH 
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   19-FEB-2014, entry version 64.
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   PATRIC; 32329647; VBISalEnt136302_4738.
DR   eggNOG; COG1974; -.
DR   OMA; QNTANNG; -.
DR   OrthoDB; EOG6JHRHJ; -.
DR   ProtClustDB; PRK00215; -.
DR   BioCyc; SENT321314:GJCS-4312-MONOMER; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-HAMAP.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006351; P:transcription, DNA-templated; 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; IPR006200; LexA.
DR   InterPro; IPR006199; LexA_DNA-bd_dom.
DR   InterPro; IPR028360; Peptidase_S24/S26_b-rbn.
DR   InterPro; IPR006197; Peptidase_S24_LexA.
DR   InterPro; IPR019759; Peptidase_S24_S26.
DR   InterPro; IPR015927; Peptidase_S24_S26A/B/C.
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; SSF51306; 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
//
DBGET integrated database retrieval system