(data stored in ACNUC7421 zone)

SWISSPROT: LEXA_EDWI9

ID   LEXA_EDWI9              Reviewed;         202 AA.
AC   C5B718;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 55.
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=NT01EI_0237;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) 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. 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. {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; CP001600; ACR67480.1; -; Genomic_DNA.
DR   RefSeq; WP_015869689.1; NC_012779.2.
DR   SMR; C5B718; -.
DR   STRING; 634503.NT01EI_0237; -.
DR   MEROPS; S24.001; -.
DR   EnsemblBacteria; ACR67480; ACR67480; NT01EI_0237.
DR   GeneID; 7960018; -.
DR   KEGG; eic:NT01EI_0237; -.
DR   PATRIC; fig|634503.3.peg.213; -.
DR   eggNOG; ENOG4105DS7; Bacteria.
DR   eggNOG; COG1974; LUCA.
DR   HOGENOM; HOG000232167; -.
DR   KO; K01356; -.
DR   OMA; RQMMQAM; -.
DR   OrthoDB; POG091H029U; -.
DR   Proteomes; UP000001485; 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; C5B718.
DR   SWISS-2DPAGE; C5B718.
KW   Autocatalytic cleavage; Complete proteome; DNA damage; DNA repair;
KW   DNA replication; DNA-binding; Hydrolase; Reference proteome;
KW   Repressor; SOS response; Transcription; Transcription regulation.
FT   CHAIN         1    202       LexA repressor.
FT                                /FTId=PRO_1000201820.
FT   DNA_BIND     28     48       H-T-H motif. {ECO:0000255|HAMAP-
FT                                Rule:MF_00015}.
FT   ACT_SITE    119    119       For autocatalytic cleavage activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00015}.
FT   ACT_SITE    156    156       For autocatalytic cleavage activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_00015}.
FT   SITE         84     85       Cleavage; by autolysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_00015}.
SQ   SEQUENCE   202 AA;  22428 MW;  D3DF1EAC155D7EDD CRC64;
     MKALTARQQQ VYDLIRDHIE QTGMPPTRAE IAQRLGFRSP NAAEEHLKAL QRKGVIEIVS
     GASRGIRLLM EDETGLPLVG QVAAGEPLLA QQHIEGFYQI DPSLFKPGAD FLLRVNGMSM
     RDIGILDGDL LAVHKTQDVR NGQVVVARIE DEVTVKRLKK QGNMVQLLPE NCDFQPIVVD
     LREQSFTIEG LAVGVIRNGD WI
//

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