LEXA_MYCTU
ID LEXA_MYCTU Reviewed; 236 AA.
AC P9WHR7; L0TD53; O08191; Q50765;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
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=Rv2720;
GN ORFNames=MTCY05A6.41;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DNA-BINDING SPECIFICITY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9084177; DOI=10.1099/00221287-143-3-929;
RA Movahedzadeh F., Colston M.J., Davis E.O.;
RT "Characterization of Mycobacterium tuberculosis LexA: recognition of a Cheo
RT (Bacillus-type SOS) box.";
RL Microbiology 143:929-936(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP START SITE IDENTIFICATION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19118359; DOI=10.1099/mic.0.022889-0;
RA Smollett K.L., Fivian-Hughes A.S., Smith J.E., Chang A., Rao T.,
RA Davis E.O.;
RT "Experimental determination of translational start sites resolves
RT uncertainties in genomic open reading frame predictions - application to
RT Mycobacterium tuberculosis.";
RL Microbiology 155:186-197(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Represses a number of genes involved in the response to DNA
CC damage (SOS response), including recA and lexA. Has been shown to bind
CC to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'. In the presence
CC of single-stranded DNA, RecA interacts with LexA causing an
CC autocatalytic cleavage which disrupts the DNA-binding part of LexA,
CC leading to derepression of the SOS regulon and eventually DNA repair.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA62750.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X91407; CAA62750.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL123456; CCP45518.1; -; Genomic_DNA.
DR PIR; C70533; C70533.
DR RefSeq; NP_217236.2; NC_000962.3.
DR RefSeq; WP_003899448.1; NZ_NVQJ01000017.1.
DR PDB; 6A2Q; X-ray; 1.48 A; A=126-236.
DR PDB; 6A2R; X-ray; 2.25 A; A/B/C/D/E/F=126-236.
DR PDB; 6A2S; X-ray; 2.50 A; A/B/C/D/E/F/G/H=126-236.
DR PDB; 6A2T; X-ray; 1.90 A; A=126-236.
DR PDBsum; 6A2Q; -.
DR PDBsum; 6A2R; -.
DR PDBsum; 6A2S; -.
DR PDBsum; 6A2T; -.
DR AlphaFoldDB; P9WHR7; -.
DR SMR; P9WHR7; -.
DR STRING; 83332.Rv2720; -.
DR MEROPS; S24.001; -.
DR PaxDb; P9WHR7; -.
DR DNASU; 888169; -.
DR GeneID; 45426707; -.
DR GeneID; 888169; -.
DR KEGG; mtu:Rv2720; -.
DR TubercuList; Rv2720; -.
DR eggNOG; COG1974; Bacteria.
DR BRENDA; 3.4.21.88; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0003677; F:DNA binding; IDA:MTBBASE.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:MTBBASE.
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; IDA:MTBBASE.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEP:MTBBASE.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
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 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; DNA damage; DNA repair;
KW DNA replication; DNA-binding; Hydrolase; Reference proteome; Repressor;
KW SOS response; Transcription; Transcription regulation.
FT CHAIN 1..236
FT /note="LexA repressor"
FT /id="PRO_0000170059"
FT DNA_BIND 51..71
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 160
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT ACT_SITE 197
FT /note="For autocatalytic cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT SITE 125..126
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00015"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:6A2S"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:6A2Q"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:6A2Q"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:6A2Q"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:6A2Q"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:6A2Q"
FT STRAND 193..202
FT /evidence="ECO:0007829|PDB:6A2Q"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:6A2Q"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:6A2Q"
FT STRAND 223..233
FT /evidence="ECO:0007829|PDB:6A2Q"
SQ SEQUENCE 236 AA; 24841 MW; BF88E0D234B3A051 CRC64;
MNDSNDTSVA GGAAGADSRV LSADSALTER QRTILDVIRA SVTSRGYPPS IREIGDAVGL
TSTSSVAHQL RTLERKGYLR RDPNRPRAVN VRGADDAALP PVTEVAGSDA LPEPTFVPVL
GRIAAGGPIL AEEAVEDVFP LPRELVGEGT LFLLKVIGDS MVEAAICDGD WVVVRQQNVA
DNGDIVAAMI DGEATVKTFK RAGGQVWLMP HNPAFDPIPG NDATVLGKVV TVIRKV
