MLRA_ECOLI
ID MLRA_ECOLI Reviewed; 243 AA.
AC P33358; Q2MAV3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=HTH-type transcriptional regulator MlrA {ECO:0000305};
DE AltName: Full=MerR-like regulator A {ECO:0000303|PubMed:11489123};
GN Name=mlrA {ECO:0000303|PubMed:11489123}; Synonyms=yehV;
GN OrderedLocusNames=b2127, JW2115;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33694 / HB101, and Chi7122;
RX PubMed=11489123; DOI=10.1046/j.1365-2958.2001.02529.x;
RA Brown P.K., Dozois C.M., Nickerson C.A., Zuppardo A., Terlonge J.,
RA Curtiss R. III;
RT "MlrA, a novel regulator of curli (AgF) and extracellular matrix synthesis
RT by Escherichia coli and Salmonella enterica serovar Typhimurium.";
RL Mol. Microbiol. 41:349-363(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RT "Automated multiplex sequencing of the E.coli genome.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=20874755; DOI=10.1111/j.1574-6968.2010.02112.x;
RA Ogasawara H., Yamamoto K., Ishihama A.;
RT "Regulatory role of MlrA in transcription activation of csgD, the master
RT regulator of biofilm formation in Escherichia coli.";
RL FEMS Microbiol. Lett. 312:160-168(2010).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH DGCM AND PDER.
RX PubMed=23708798; DOI=10.1038/emboj.2013.120;
RA Lindenberg S., Klauck G., Pesavento C., Klauck E., Hengge R.;
RT "The EAL domain protein YciR acts as a trigger enzyme in a c-di-GMP
RT signalling cascade in E. coli biofilm control.";
RL EMBO J. 32:2001-2014(2013).
CC -!- FUNCTION: Activates transcription of csgD, the master regulator of
CC biofilm formation, by binding to its promoter region (PubMed:11489123,
CC PubMed:20874755). Also controls the transcription of cadC and ibaG
CC (PubMed:20874755). Part of a signaling cascade that regulates curli
CC biosynthesis. The cascade is composed of two c-di-GMP control modules,
CC in which c-di-GMP controlled by the DgcE/PdeH pair (module I) regulates
CC the activity of the DgcM/PdeR pair (module II), which in turn regulates
CC activity of the transcription factor MlrA (PubMed:23708798).
CC {ECO:0000269|PubMed:11489123, ECO:0000269|PubMed:20874755,
CC ECO:0000269|PubMed:23708798}.
CC -!- ACTIVITY REGULATION: Activity is regulated by DgcM and PdeR.
CC {ECO:0000269|PubMed:23708798}.
CC -!- SUBUNIT: Interacts with DgcM and PdeR. {ECO:0000269|PubMed:23708798}.
CC -!- INTERACTION:
CC P33358; P77302: dgcM; NbExp=2; IntAct=EBI-1127668, EBI-544662;
CC P33358; P77334: pdeR; NbExp=2; IntAct=EBI-1127668, EBI-548149;
CC -!- DISRUPTION PHENOTYPE: Knockout mutant no longer produces curli, is
CC mannose-resistant haemagglutination (MRHA) negative and produces smooth
CC white colonies on Congo red agar. {ECO:0000269|PubMed:11489123}.
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DR EMBL; AF288173; AAK84657.1; -; Genomic_DNA.
DR EMBL; AF288174; AAK84658.1; -; Genomic_DNA.
DR EMBL; U00007; AAA60490.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75188.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76603.1; -; Genomic_DNA.
DR PIR; F64980; F64980.
DR RefSeq; NP_416631.1; NC_000913.3.
DR RefSeq; WP_001240401.1; NZ_STEB01000002.1.
DR AlphaFoldDB; P33358; -.
DR SMR; P33358; -.
DR BioGRID; 4260445; 16.
DR BioGRID; 853273; 1.
DR IntAct; P33358; 9.
DR MINT; P33358; -.
DR STRING; 511145.b2127; -.
DR jPOST; P33358; -.
DR PaxDb; P33358; -.
DR PRIDE; P33358; -.
DR EnsemblBacteria; AAC75188; AAC75188; b2127.
DR EnsemblBacteria; BAE76603; BAE76603; BAE76603.
DR GeneID; 66673978; -.
DR GeneID; 949029; -.
DR KEGG; ecj:JW2115; -.
DR KEGG; eco:b2127; -.
DR PATRIC; fig|1411691.4.peg.118; -.
DR EchoBASE; EB1946; -.
DR eggNOG; COG0789; Bacteria.
DR HOGENOM; CLU_045945_0_1_6; -.
DR InParanoid; P33358; -.
DR OMA; EQGWRVD; -.
DR PhylomeDB; P33358; -.
DR BioCyc; EcoCyc:EG12008-MON; -.
DR PRO; PR:P33358; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:EcoCyc.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR000551; MerR-type_HTH_dom.
DR Pfam; PF13411; MerR_1; 1.
DR SMART; SM00422; HTH_MERR; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
DR PROSITE; PS00552; HTH_MERR_1; 1.
DR PROSITE; PS50937; HTH_MERR_2; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..243
FT /note="HTH-type transcriptional regulator MlrA"
FT /id="PRO_0000098144"
FT DOMAIN 3..72
FT /note="HTH merR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00254"
FT DNA_BIND 6..25
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00254"
SQ SEQUENCE 243 AA; 28046 MW; 48F6D16051C04319 CRC64;
MALYTIGEVA LLCDINPVTL RAWQRRYGLL KPQRTDGGHR LFNDADIDRI REIKRWIDNG
VQVSKVKMLL SNENVDVQNG WRDQQETLLT YLQSGNLHSL RTWIKERGQD YPAQTLTTHL
FIPLRRRLQC QQPTLQALLA ILDGVLINYI AICLASARKK QGKDALVVGW NIQDTTRLWL
EGWIASQQGW RIDVLAHSLN QLRPELFEGR TLLVWCGENR TSAQQQQLTS WQEQGHDIFP
LGI
