(data stored in ACNUC7421 zone)

SWISSPROT: LEXA_SHESH

ID   LEXA_SHESH              Reviewed;         206 AA.
AC   A8FPP0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 72.
DE   RecName: Full=LexA repressor {ECO:0000255|HAMAP-Rule:MF_00015};
DE            EC=3.4.21.88 {ECO:0000255|HAMAP-Rule:MF_00015};
GN   Name=lexA {ECO:0000255|HAMAP-Rule:MF_00015};
GN   OrderedLocusNames=Ssed_0200;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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. {ECO:0000255|HAMAP-Rule:MF_00015}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of Ala-|-Gly bond in repressor
CC       LexA. {ECO:0000255|HAMAP-Rule:MF_00015}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00015}.
CC   -!- SIMILARITY: Belongs to the peptidase S24 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00015}.
DR   EMBL; CP000821; ABV34813.1; -; Genomic_DNA.
DR   RefSeq; WP_012004339.1; NC_009831.1.
DR   ProteinModelPortal; A8FPP0; -.
DR   SMR; A8FPP0; -.
DR   STRING; 425104.Ssed_0200; -.
DR   MEROPS; S24.001; -.
DR   EnsemblBacteria; ABV34813; ABV34813; Ssed_0200.
DR   KEGG; sse:Ssed_0200; -.
DR   eggNOG; ENOG4105DS7; Bacteria.
DR   eggNOG; COG1974; LUCA.
DR   HOGENOM; HOG000232167; -.
DR   KO; K01356; -.
DR   OMA; RQMMQAM; -.
DR   OrthoDB; POG091H029U; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   HAMAP; MF_00015; LexA; 1.
DR   InterPro; IPR006200; LexA.
DR   InterPro; IPR006199; LexA_DNA-bd_dom.
DR   InterPro; IPR006197; Peptidase_S24_LexA.
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; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF51306; SSF51306; 1.
DR   TIGRFAMs; TIGR00498; lexA; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FPP0.
DR   SWISS-2DPAGE; A8FPP0.
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    206       LexA repressor.
FT                                /FTId=PRO_1000074067.
FT   DNA_BIND     28     48       H-T-H motif. {ECO:0000255|HAMAP-
FT                                Rule:MF_00015}.
FT   ACT_SITE    123    123       For autocatalytic cleavage activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00015}.
FT   ACT_SITE    160    160       For autocatalytic cleavage activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00015}.
FT   SITE         88     89       Cleavage; by autolysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_00015}.
SQ   SEQUENCE   206 AA;  22636 MW;  8995A0A85C2F74EA CRC64;
     MRPLTPRQAE ILELIKRNIA DTGMPPTRAE IAKRLGFKSA NAAEEHLKAL AKKGCIEIIP
     GTSRGIRLTQ ANESEEELGL PLIGQVAAGE PILAQEHVEQ HYQIDPAMFR PSADFLLRVR
     GDSMKNIGIL EGDLLAVHKA EQARNGQVVV ARVEDDVTVK RFEKKGSIVY LHAENEDYSP
     IVVDLTSESL SIEGLAVGVI RNGDWQ
//

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