ID A0A1F5H358_9BACT Unreviewed; 212 AA.
AC A0A1F5H358;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Repressor LexA {ECO:0000313|EMBL:OGD98487.1};
GN ORFNames=A3B54_04465 {ECO:0000313|EMBL:OGD98487.1};
OS Candidatus Curtissbacteria bacterium RIFCSPLOWO2_01_FULL_42_50.
OC Bacteria; Candidatus Curtissbacteria.
OX NCBI_TaxID=1797730 {ECO:0000313|EMBL:OGD98487.1, ECO:0000313|Proteomes:UP000177039};
RN [1] {ECO:0000313|EMBL:OGD98487.1, ECO:0000313|Proteomes:UP000177039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SIMILARITY: Belongs to the peptidase S24 family.
CC {ECO:0000256|ARBA:ARBA00007484, ECO:0000256|RuleBase:RU003991}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGD98487.1}.
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DR EMBL; MFBT01000036; OGD98487.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5H358; -.
DR Proteomes; UP000177039; Unassembled WGS sequence.
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 DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
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 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,
KW ECO:0000256|RuleBase:RU003991}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003991};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW SOS response {ECO:0000256|ARBA:ARBA00023236};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 4..65
FT /note="LexA repressor DNA-binding"
FT /evidence="ECO:0000259|Pfam:PF01726"
FT DOMAIN 84..199
FT /note="Peptidase S24/S26A/S26B/S26C"
FT /evidence="ECO:0000259|Pfam:PF00717"
SQ SEQUENCE 212 AA; 23816 MW; 72E642E3B75F96D7 CRC64;
MNLPITPRQK QMLSIIYNYI KNSGYPPTFE EMKNRLGVSS NQSVLDLLNK LEEKKAIKRN
ESVARSIAIL PLGYEILDNP PLVPFLGLSH AGSPMEAIQI EGEWQPLSSN VAKLEEEVFL
LKVSGDSMIN AGIDDGDLVL VKRHKEFVSG DIVLARIGDD VTIKRFVSED KPPYLYLKPE
NPSYEIIHFT EDVVLDGKVI SILKNGQWRP TL
//
