ID A0A0U1EDT3_STACP Unreviewed; 206 AA.
AC A0A0U1EDT3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 48.
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 ECO:0000313|EMBL:NMK97734.1};
GN ORFNames=EQ811_03635 {ECO:0000313|EMBL:TBW78173.1}, HHM13_06450
GN {ECO:0000313|EMBL:NMK97734.1}, NCTC11045_01518
GN {ECO:0000313|EMBL:VTR17119.1};
OS Staphylococcus capitis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=29388 {ECO:0000313|EMBL:NMK97734.1, ECO:0000313|Proteomes:UP000550736};
RN [1] {ECO:0000313|EMBL:TBW78173.1, ECO:0000313|Proteomes:UP000291949}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H8 {ECO:0000313|EMBL:TBW78173.1,
RC ECO:0000313|Proteomes:UP000291949};
RA Williams M.R.;
RT "Quorum sensing between bacterial species on the skin protects against
RT epidermal injury in atopic dermatitis.";
RL Sci. Transl. Med. 0:0-0(2019).
RN [2] {ECO:0000313|EMBL:VTR17119.1, ECO:0000313|Proteomes:UP000403553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC11045 {ECO:0000313|EMBL:VTR17119.1,
RC ECO:0000313|Proteomes:UP000403553};
RG Pathogen Informatics;
RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:NMK97734.1, ECO:0000313|Proteomes:UP000550736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12-86 {ECO:0000313|EMBL:NMK97734.1,
RC ECO:0000313|Proteomes:UP000550736};
RA Ding L., Li P., Yang Y., Lin D., Xu X.;
RT "The Epidemiology and Molecular Characteristics of Linezolid-Resistant
RT Staphylococcus capitis in Huashan Hospital, Shanghai.";
RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
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; JABBLX010000012; NMK97734.1; -; Genomic_DNA.
DR EMBL; SCHC01000001; TBW78173.1; -; Genomic_DNA.
DR EMBL; CABEEX010000003; VTR17119.1; -; Genomic_DNA.
DR RefSeq; WP_002433936.1; NZ_WHVU01000001.1.
DR AlphaFoldDB; A0A0U1EDT3; -.
DR GeneID; 77313805; -.
DR eggNOG; COG1974; Bacteria.
DR Proteomes; UP000291949; Unassembled WGS sequence.
DR Proteomes; UP000403553; Unassembled WGS sequence.
DR Proteomes; UP000550736; Unassembled WGS sequence.
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:UniProtKB-KW.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR CDD; cd00090; HTH_ARSR; 1.
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; IPR011991; ArsR-like_HTH.
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 Protease {ECO:0000313|EMBL:VTR17119.1};
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 1..65
FT /note="LexA repressor DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF01726"
FT DOMAIN 85..200
FT /note="Peptidase S24/S26A/S26B/S26C"
FT /evidence="ECO:0000259|Pfam:PF00717"
FT DNA_BIND 28..48
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT ACT_SITE 129
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT ACT_SITE 167
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT SITE 92..93
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
SQ SEQUENCE 206 AA; 23248 MW; B7CC15106D9195CB CRC64;
MRELTKRQSE IYDYIKHIVQ TKGYPPSVRE IGEAVGLASS STVHGHLSRL EEKGYIRRDP
TKPRAIEIVS EQLEEVNVEE TIHVPVIGKV TAGVPITAVE NIEEYFPLPE HLTSTHNSDI
FILNVVGESM IEAGILDGDK VIVRSQTIAE NGDIIVAMTE DEEATVKRFY KEKNRYRLQP
ENSTMDPIYL DNVIVVGKVI GLYREM
//