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Database: UniProt
Entry: B7KUX3_METC4
LinkDB: B7KUX3_METC4
Original site: B7KUX3_METC4 
ID   B7KUX3_METC4            Unreviewed;       240 AA.
AC   B7KUX3;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   24-JAN-2024, entry version 101.
DE   RecName: Full=LexA repressor {ECO:0000256|HAMAP-Rule:MF_00015};
DE            EC=3.4.21.88 {ECO:0000256|HAMAP-Rule:MF_00015};
GN   Name=lexA {ECO:0000256|HAMAP-Rule:MF_00015};
GN   OrderedLocusNames=Mchl_5148 {ECO:0000313|EMBL:ACK85912.1};
OS   Methylorubrum extorquens (strain CM4 / NCIMB 13688) (Methylobacterium
OS   extorquens).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=440085 {ECO:0000313|EMBL:ACK85912.1, ECO:0000313|Proteomes:UP000002385};
RN   [1] {ECO:0000313|Proteomes:UP000002385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM4 / NCIMB 13688 {ECO:0000313|Proteomes:UP000002385};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Marx C., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium chloromethanicum
RT   CM4.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACK85912.1, ECO:0000313|Proteomes:UP000002385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM4 / NCIMB 13688 {ECO:0000313|Proteomes:UP000002385};
RX   PubMed=22887658; DOI=10.1128/JB.01009-12;
RA   Marx C.J., Bringel F., Chistoserdova L., Moulin L., Farhan Ul Haque M.,
RA   Fleischman D.E., Gruffaz C., Jourand P., Knief C., Lee M.C., Muller E.E.,
RA   Nadalig T., Peyraud R., Roselli S., Russ L., Goodwin L.A., Ivanova N.,
RA   Kyrpides N., Lajus A., Land M.L., Medigue C., Mikhailova N., Nolan M.,
RA   Woyke T., Stolyar S., Vorholt J.A., Vuilleumier S.;
RT   "Complete genome sequences of six strains of the genus Methylobacterium.";
RL   J. Bacteriol. 194:4746-4748(2012).
CC   -!- FUNCTION: Represses a number of genes involved in the response to DNA
CC       damage (SOS response), including recA and lexA. In the presence of
CC       single-stranded DNA, RecA interacts with LexA causing an autocatalytic
CC       cleavage which disrupts the DNA-binding part of LexA, leading to
CC       derepression of the SOS regulon and eventually DNA repair.
CC       {ECO:0000256|HAMAP-Rule:MF_00015}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of Ala-|-Gly bond in repressor LexA.; EC=3.4.21.88;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00015};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00015}.
CC   -!- SIMILARITY: Belongs to the peptidase S24 family.
CC       {ECO:0000256|ARBA:ARBA00007484, ECO:0000256|HAMAP-Rule:MF_00015,
CC       ECO:0000256|RuleBase:RU003991}.
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DR   EMBL; CP001298; ACK85912.1; -; Genomic_DNA.
DR   RefSeq; WP_003603900.1; NC_011757.1.
DR   AlphaFoldDB; B7KUX3; -.
DR   MEROPS; S24.001; -.
DR   GeneID; 72992416; -.
DR   KEGG; mch:Mchl_5148; -.
DR   HOGENOM; CLU_066192_45_2_5; -.
DR   OMA; HVWLLPH; -.
DR   Proteomes; UP000002385; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR   CDD; cd06529; S24_LexA-like; 1.
DR   Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   HAMAP; MF_00015; LexA; 1.
DR   InterPro; IPR006200; LexA.
DR   InterPro; IPR039418; LexA-like.
DR   InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR   InterPro; IPR006199; LexA_DNA-bd_dom.
DR   InterPro; IPR006197; Peptidase_S24_LexA.
DR   InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   NCBIfam; TIGR00498; lexA; 1.
DR   PANTHER; PTHR33516; LEXA REPRESSOR; 1.
DR   PANTHER; PTHR33516:SF2; LEXA REPRESSOR; 1.
DR   Pfam; PF01726; LexA_DNA_bind; 1.
DR   Pfam; PF00717; Peptidase_S24; 1.
DR   PRINTS; PR00726; LEXASERPTASE.
DR   SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813, ECO:0000256|HAMAP-
KW   Rule:MF_00015};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00015};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00015};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_00015};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00015};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00015};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|HAMAP-Rule:MF_00015};
KW   SOS response {ECO:0000256|ARBA:ARBA00023236, ECO:0000256|HAMAP-
KW   Rule:MF_00015};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00015};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW   Rule:MF_00015}.
FT   DOMAIN          2..63
FT                   /note="LexA repressor DNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01726"
FT   DOMAIN          119..234
FT                   /note="Peptidase S24/S26A/S26B/S26C"
FT                   /evidence="ECO:0000259|Pfam:PF00717"
FT   DNA_BIND        26..46
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT   REGION          74..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        161
FT                   /note="For autocatalytic cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT   ACT_SITE        199
FT                   /note="For autocatalytic cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT   SITE            126..127
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
SQ   SEQUENCE   240 AA;  26333 MW;  D2664448D6BD0877 CRC64;
     MLTRKQLELL QFIQQRMQES GVPPSFDEMK DALDLKSKSG IHRLIMALEE RGFLRRLPNR
     ARAIEILRMP DMPAAKPASS EPRRFTPSVV EGGLSAKPAA PKPPMLQAHD GKGQSVMVPV
     MGRIAAGVPI SAIESQSHSI SMSPDFLSGG EHYALEVRGD SMIEAGILDG DLVVIHKQET
     ANNGDIIVAL IDDEEATLKR LRRRGSSIAL EAANPAYETR VLGPDRVRIQ GKLVSLVRRY
//
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