LEXA_SYNY3
ID LEXA_SYNY3 Reviewed; 203 AA.
AC P73722;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Transcription regulator LexA;
DE AltName: Full=LexA-related repressor {ECO:0000303|PubMed:16840531};
GN Name=lexA; OrderedLocusNames=sll1626;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=15225304; DOI=10.1111/j.1365-2958.2004.04100.x;
RA Domain F., Houot L., Chauvat F., Cassier-Chauvat C.;
RT "Function and regulation of the cyanobacterial genes lexA, recA and ruvB:
RT LexA is critical to the survival of cells facing inorganic carbon
RT starvation.";
RL Mol. Microbiol. 53:65-80(2004).
RN [3]
RP FUNCTION, AND DNA-BINDING.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=16102913; DOI=10.1016/j.femsle.2005.07.024;
RA Oliveira P., Lindblad P.;
RT "LexA, a transcription regulator binding in the promoter region of the
RT bidirectional hydrogenase in the cyanobacterium Synechocystis sp. PCC
RT 6803.";
RL FEMS Microbiol. Lett. 251:59-66(2005).
RN [4]
RP FUNCTION, SUBUNIT, DOMAIN, DISRUPTION PHENOTYPE, AND DNA-BINDING.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=16238629; DOI=10.1111/j.1365-2958.2005.04867.x;
RA Gutekunst K., Phunpruch S., Schwarz C., Schuchardt S., Schulz-Friedrich R.,
RA Appel J.;
RT "LexA regulates the bidirectional hydrogenase in the cyanobacterium
RT Synechocystis sp. PCC 6803 as a transcription activator.";
RL Mol. Microbiol. 58:810-823(2005).
RN [5]
RP FUNCTION, INDUCTION, AND DNA-BINDING.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=16840531; DOI=10.1093/nar/gkl426;
RA Patterson-Fortin L.M., Colvin K.R., Owttrim G.W.;
RT "A LexA-related protein regulates redox-sensitive expression of the
RT cyanobacterial RNA helicase, crhR.";
RL Nucleic Acids Res. 34:3446-3454(2006).
RN [6]
RP FUNCTION, SUBUNIT, AND DNA-BINDING.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=18555801; DOI=10.1016/j.febslet.2008.06.009;
RA Patterson-Fortin L.M., Owttrim G.W.;
RT "A Synechocystis LexA-orthologue binds direct repeats in target genes.";
RL FEBS Lett. 582:2424-2430(2008).
RN [7]
RP SUBCELLULAR LOCATION, INDUCTION, AND POST-TRANSLATIONAL MODIFICATION.
RX PubMed=21642463; DOI=10.1128/jb.00289-11;
RA Oliveira P., Lindblad P.;
RT "Novel insights into the regulation of LexA in the cyanobacterium
RT Synechocystis sp. Strain PCC 6803.";
RL J. Bacteriol. 193:3804-3814(2011).
CC -!- FUNCTION: A probable transcription regulator, probably involved in
CC carbon metabolism (PubMed:15225304). Binds and probably regulates
CC expression of bidirectional hydrogenase (hoxEFUHY), probably activates
CC its transcription (PubMed:16102913, PubMed:16238629). A possible
CC regulator of redox-responsive genes. Binds 2 direct repeats of the DNA
CC with sequence 5'-CTA-N(9)-CTA-3' in the upstream region of both its own
CC gene (includes the transcription start site) and crhR (includes the
CC initiation codon) in a sequence-specific manner; does not bind crhR RNA
CC (PubMed:18555801). Binds to the crhR gene, represses its transcription
CC (PubMed:16840531). {ECO:0000269|PubMed:15225304,
CC ECO:0000269|PubMed:16102913, ECO:0000269|PubMed:16238629,
CC ECO:0000269|PubMed:16840531, ECO:0000269|PubMed:18555801}.
CC -!- SUBUNIT: Monomer in solution, probably binds DNA as a dimer.
CC {ECO:0000269|PubMed:18555801, ECO:0000305|PubMed:16238629}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21642463}.
CC Note=Localized in the innermost region of the cytoplasm, associated
CC with DNA in an evenly distributed pattern no changes are seen when
CC cells are grown in the dark. {ECO:0000269|PubMed:21642463}.
CC -!- INDUCTION: Expressed in light grown cells, strongly repressed post-
CC transcriptionally by UV-C light, repressed by H(2)O(2) and SeO(3) but
CC not by SeO(4) (PubMed:15225304). Strongly expressed in dark-grown
CC cells, induced in light-grown cells by glucose, repressed at 20 degrees
CC Celsius (PubMed:16840531). Not induced following UV light exposure
CC between 150 and 600 J/m(2), suggesting it does not respond to DNA
CC damage (PubMed:15225304). Despite changes in transcript levels, protein
CC levels are constant under light-dark regimes, anaerobic growth and in
CC presence of glucose (at protein level) (PubMed:21642463).
CC {ECO:0000269|PubMed:15225304, ECO:0000269|PubMed:16840531,
CC ECO:0000269|PubMed:21642463}.
CC -!- DOMAIN: The N-terminal fragment (residues 1-88) binds hox promoter DNA.
CC {ECO:0000269|PubMed:16238629}.
CC -!- PTM: 5 protein spots of the same molecular weight but different pI are
CC seen in vivo; all of them bind DNA. {ECO:0000269|PubMed:21642463}.
CC -!- DISRUPTION PHENOTYPE: Probably essential, it cannot be deleted
CC (PubMed:15225304). Depleted strain have decreased levels of hox
CC hydrogenase (PubMed:16102913). In depletion studies using merodiploid
CC strains 32 genes are up-regulated while 25 are down-regulated; many of
CC them are known or predicted to be involved in carbon metabolism; cells
CC grow poorly in the absence of inorganic carbon (PubMed:15225304).
CC {ECO:0000269|PubMed:15225304, ECO:0000269|PubMed:16102913}.
CC -!- MISCELLANEOUS: This bacterium is considerably more resistant to UV and
CC gamma irradiation than E.coli; the E.coli-like SOS regulon model is not
CC an appropriate model for DNA repair in this cyanobacterium.
CC {ECO:0000305|PubMed:15225304}.
CC -!- SIMILARITY: Belongs to the peptidase S24 family. {ECO:0000305}.
CC -!- CAUTION: Does not encode the amino acids known to be needed in E.coli
CC for autocatalytic cleavage, probably acts differently from E.coli LexA.
CC {ECO:0000305|PubMed:16840531}.
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DR EMBL; BA000022; BAA17770.1; -; Genomic_DNA.
DR PIR; S74809; S74809.
DR AlphaFoldDB; P73722; -.
DR SMR; P73722; -.
DR STRING; 1148.1652852; -.
DR PaxDb; P73722; -.
DR EnsemblBacteria; BAA17770; BAA17770; BAA17770.
DR KEGG; syn:sll1626; -.
DR eggNOG; COG1974; Bacteria.
DR InParanoid; P73722; -.
DR OMA; HVWLLPH; -.
DR PhylomeDB; P73722; -.
DR Proteomes; UP000001425; Chromosome.
DR CollecTF; EXPREG_00000be0; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF.
DR GO; GO:0043565; F:sequence-specific DNA binding; IMP:CollecTF.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:CollecTF.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEP:CollecTF.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0009432; P:SOS response; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR006200; LexA.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR006199; LexA_DNA-bd_dom.
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 SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF51306; SSF51306; 1.
DR TIGRFAMs; TIGR00498; lexA; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; DNA replication; DNA-binding; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..203
FT /note="Transcription regulator LexA"
FT /id="PRO_0000434786"
FT REGION 1..88
FT /note="Binds hox promoter DNA"
FT /evidence="ECO:0000269|PubMed:16238629"
SQ SEQUENCE 203 AA; 22744 MW; 27E92C9163B4E19C CRC64;
MEPLTRAQKE LFDWLVSYID ETQHAPSIRQ MMRAMNLRSP APIQSRLERL RNKGYVDWTD
GKARTLRILH QKPKGVSVIG ELKGGELVEA DAEEVEKIDF APLMKKSSVF ALRVMSNDLV
DDFIVEGDML ILRSVTGEEE IEDGELVAAS IKGGKIAIKR YYQDGTKVVL KASNNKGPGQ
ELKASDVEIQ GILMGVWRNF QGV
