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Database: UniProt/SWISS-PROT
Entry: LEXA_STRM5
LinkDB: LEXA_STRM5
Original site: LEXA_STRM5 
ID   LEXA_STRM5              Reviewed;         211 AA.
AC   B4SRA9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   14-MAY-2014, entry version 45.
DE   RecName: Full=LexA repressor;
DE            EC=3.4.21.88;
GN   Name=lexA; OrderedLocusNames=Smal_1475;
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) 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; CP001111; ACF51180.1; -; Genomic_DNA.
DR   RefSeq; YP_002027863.1; NC_011071.1.
DR   ProteinModelPortal; B4SRA9; -.
DR   STRING; 391008.Smal_1475; -.
DR   MEROPS; S24.001; -.
DR   EnsemblBacteria; ACF51180; ACF51180; Smal_1475.
DR   GeneID; 6475339; -.
DR   KEGG; smt:Smal_1475; -.
DR   PATRIC; 23707884; VBISteMal40512_1501.
DR   eggNOG; COG1974; -.
DR   HOGENOM; HOG000232167; -.
DR   KO; K01356; -.
DR   OMA; YIEWTEG; -.
DR   OrthoDB; EOG6JHRHJ; -.
DR   BioCyc; SMAL391008:GH1H-1521-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: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    211       LexA repressor.
FT                                /FTId=PRO_1000089600.
FT   DNA_BIND     27     47       H-T-H motif (By similarity).
FT   ACT_SITE    131    131       For autocatalytic cleavage activity (By
FT                                similarity).
FT   ACT_SITE    168    168       For autocatalytic cleavage activity (By
FT                                similarity).
FT   SITE         96     97       Cleavage; by autolysis (By similarity).
SQ   SEQUENCE   211 AA;  23159 MW;  099573DCA48A1BD5 CRC64;
     MDLTDTQQAI LQLIAERIES EGAPPSQTEI ARAFGFKGVR AAQYHLEALE QAGAIRRIPG
     QARGIRLVQA PPLEKLAEPG LPDNVLRLPV LGRVAAGLPI GADIGSDDFV VLDRVFFSPA
     PDYLLKVQGD SMIDEGIFDG DLIGVHRTRD AHSGQIVVAR IDDEITVKLL KIAKDRIRLL
     PRNPDYKPIE VLPDQDFSIE GLYCGLLRPN R
//
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