LEXA_PSEAE
ID LEXA_PSEAE Reviewed; 204 AA.
AC P37452;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 146.
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}; OrderedLocusNames=PA3007;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PAO;
RX PubMed=1494343; DOI=10.1007/bf00279651;
RA Garriga X., Calero S., Barbe J.;
RT "Nucleotide sequence analysis and comparison of the lexA genes from
RT Salmonella typhimurium, Erwinia carotovora, Pseudomonas aeruginosa and
RT Pseudomonas putida.";
RL Mol. Gen. Genet. 236:125-134(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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:0000255|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:0000255|HAMAP-Rule:MF_00015};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00015}.
CC -!- SIMILARITY: Belongs to the peptidase S24 family. {ECO:0000255|HAMAP-
CC Rule:MF_00015}.
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DR EMBL; X63018; CAA44750.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06395.1; -; Genomic_DNA.
DR PIR; S30165; S30165.
DR RefSeq; NP_251697.1; NC_002516.2.
DR RefSeq; WP_003091196.1; NZ_QZGE01000009.1.
DR AlphaFoldDB; P37452; -.
DR SMR; P37452; -.
DR STRING; 287.DR97_4930; -.
DR MEROPS; S24.001; -.
DR PaxDb; P37452; -.
DR PRIDE; P37452; -.
DR DNASU; 879875; -.
DR EnsemblBacteria; AAG06395; AAG06395; PA3007.
DR GeneID; 879875; -.
DR KEGG; pae:PA3007; -.
DR PATRIC; fig|208964.12.peg.3155; -.
DR PseudoCAP; PA3007; -.
DR HOGENOM; CLU_066192_45_3_6; -.
DR InParanoid; P37452; -.
DR OMA; HVWLLPH; -.
DR PhylomeDB; P37452; -.
DR BioCyc; PAER208964:G1FZ6-3059-MON; -.
DR BRENDA; 3.4.21.88; 5087.
DR Proteomes; UP000002438; Chromosome.
DR CollecTF; EXPREG_00000a60; -.
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 transcription, DNA-templated; EXP:CollecTF.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:PseudoCAP.
DR GO; GO:0009432; P:SOS response; EXP:CollecTF.
DR CDD; cd06529; S24_LexA-like; 1.
DR Gene3D; 1.10.10.10; -; 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 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;
KW Autocatalytic cleavage; DNA damage; DNA repair; DNA replication;
KW DNA-binding; Hydrolase; Reference proteome; Repressor; SOS response;
KW Transcription; Transcription regulation.
FT CHAIN 1..204
FT /note="LexA repressor"
FT /id="PRO_0000170067"
FT DNA_BIND 28..48
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT ACT_SITE 125
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT ACT_SITE 162
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT SITE 90..91
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
SQ SEQUENCE 204 AA; 22506 MW; 665DF87928D48E94 CRC64;
MQKLTPRQAE ILSFIKRCLE DHGFPPTRAE IAQELGFKSP NAAEEHLKAL ARKGAIEMTP
GASRGIRIPG FEPHAANDDE GLPVIGRVAA GAPILAEQNI EESCRINPAF FNPRADYLLR
VRGMSMKDIG ILDGDLLAVH VTREARNGQV VVARIGEEVT VKRFKREGSK VWLLAENPEF
APIEVDLKEQ ELIIEGLSVG VIRR
