ID L7NK08_PHODP Unreviewed; 208 AA.
AC L7NK08;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 63.
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:AEU10127.1};
GN ORFNames=IC627_00525 {ECO:0000313|EMBL:QOD56624.1}, PDP_0386
GN {ECO:0000313|EMBL:AEU10127.1}, PDPJ_1_01238
GN {ECO:0000313|EMBL:GAW43824.1};
OS Photobacterium damsela subsp. piscicida (causative agent of fish
OS pasteurellosis) (Pasteurella piscicida).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=38294 {ECO:0000313|EMBL:AEU10127.1};
RN [1] {ECO:0000313|EMBL:AEU10127.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NCIMB 2058 {ECO:0000313|EMBL:AEU10127.1};
RX PubMed=23219776; DOI=10.1016/j.vaccine.2012.11.064;
RA Andreoni F., Boiani R., Serafini G., Amagliani G., Dominici S.,
RA Riccioni G., Zaccone R., Mancuso M., Scapigliati G., Magnani M.;
RT "Isolation of a novel gene from Photobacterium damselae subsp. piscicida
RT and analysis of the recombinant antigen as promising vaccine candidate.";
RL Vaccine 31:820-826(2013).
RN [2] {ECO:0000313|EMBL:GAW43824.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OT-51443 {ECO:0000313|EMBL:GAW43824.1};
RA Aoki T., Teru Y., Morimoto N., Kono T., Sakai M., Takano T., Hawke J.P.,
RA Fukuda Y., Takeyama H., Hikima J.;
RT "Complete Genome Sequence of Photobacterium damselae subsp. piscicida
RT Strain OT-51443 Isolated from Yellowtail (Seriola quinqueradiata) in
RT Japan.";
RL Genome Announc. 5:e00404-17(2017).
RN [3] {ECO:0000313|Proteomes:UP000196133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT-51443 {ECO:0000313|Proteomes:UP000196133};
RA Hikima J., Teru Y., Sakai M., Takano T., Takeyama H., Aoki T.;
RT "Complete genome sequence of fish pathogenic bacteria, Photobacterium
RT damsela subsp. piscicida, strain OT-51443, isolated from yellowtail
RT (Seriola quinqueradiata) in Japan.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:QOD56624.1, ECO:0000313|Proteomes:UP000516656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS-16-0540-1 {ECO:0000313|EMBL:QOD56624.1,
RC ECO:0000313|Proteomes:UP000516656};
RA Baseggio L., Silayeva O., Buller N., Landos M., Engelstaedter J.,
RA Barnes A.C.;
RT "Complete, closed and curated genome sequences of Photobacterium damselae
RT subsp. piscicida isolates from Australia indicate localised evolution and
RT additional plasmid-borne pathogenicity mechanisms.";
RL Submitted (SEP-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; HQ599857; AEU10127.1; -; Genomic_DNA.
DR EMBL; BDMQ01000001; GAW43824.1; -; Genomic_DNA.
DR EMBL; CP061854; QOD56624.1; -; Genomic_DNA.
DR RefSeq; WP_005302475.1; NZ_SUMH01000088.1.
DR AlphaFoldDB; L7NK08; -.
DR GeneID; 57340244; -.
DR Proteomes; UP000196133; Unassembled WGS sequence.
DR Proteomes; UP000516656; Chromosome 1.
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 1..65
FT /note="LexA repressor DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF01726"
FT DOMAIN 83..199
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 125
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT ACT_SITE 162
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
FT SITE 90..91
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00015"
SQ SEQUENCE 208 AA; 22878 MW; 9FE6A1416FA016B7 CRC64;
MKPLTPRQQE VFDLIKAKIE DSGMPPTRAE IARELGFRSA NAAEEHLKAL ARKGVLEIVP
GASRGIRLLV GANDSDVEES GLPLIGQVAA GEPILAQEHV ECHYDVDPTL FKPRADFLLR
VNGMSMKNIG IMDGDLLAVH KTQDVRNGQV VVARVDDDVT VKRLDKQGRK VLLHAENEEF
DPIVVDLEHQ QLAIEGIAVG VIRNADWM
//