MARR_ECOLI
ID MARR_ECOLI Reviewed; 144 AA.
AC P27245; P76882; P77582;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 160.
DE RecName: Full=Multiple antibiotic resistance protein MarR;
GN Name=marR; Synonyms=cfxB, inaR, soxQ; OrderedLocusNames=b1530, JW5248;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8383113; DOI=10.1128/jb.175.5.1484-1492.1993;
RA Cohen S.P., Haechler H., Levy S.B.;
RT "Genetic and functional analysis of the multiple antibiotic resistance
RT (mar) locus in Escherichia coli.";
RL J. Bacteriol. 175:1484-1492(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
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 CHARACTERIZATION.
RX PubMed=8282690; DOI=10.1128/jb.176.1.143-148.1994;
RA Ariza R.R., Cohen S.P., Bachhawat N., Levy S.B., Demple B.;
RT "Repressor mutations in the marRAB operon that activate oxidative stress
RT genes and multiple antibiotic resistance in Escherichia coli.";
RL J. Bacteriol. 176:143-148(1994).
RN [6]
RP CHARACTERIZATION.
RX PubMed=7768850; DOI=10.1128/jb.177.12.3414-3419.1995;
RA Seoane A.S., Levy S.B.;
RT "Characterization of MarR, the repressor of the multiple antibiotic
RT resistance (mar) operon in Escherichia coli.";
RL J. Bacteriol. 177:3414-3419(1995).
RN [7]
RP MUTAGENESIS.
RX PubMed=10760140; DOI=10.1046/j.1365-2958.2000.01802.x;
RA Alekshun M.N., Kim Y.S., Levy S.B.;
RT "Mutational analysis of MarR, the negative regulator of marRAB expression
RT in Escherichia coli, suggests the presence of two regions required for DNA
RT binding.";
RL Mol. Microbiol. 35:1394-1404(2000).
CC -!- FUNCTION: Repressor of the marRAB operon which is involved in the
CC activation of both antibiotic resistance and oxidative stress genes.
CC Binds to the marO operator/promoter site.
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DR EMBL; M96235; AAC16394.2; -; Genomic_DNA.
DR EMBL; U00096; AAC74603.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15220.1; -; Genomic_DNA.
DR PIR; E64907; E64907.
DR RefSeq; NP_416047.4; NC_000913.3.
DR RefSeq; WP_000843414.1; NZ_SSUW01000005.1.
DR PDB; 1JGS; X-ray; 2.30 A; A=7-144.
DR PDB; 3VB2; X-ray; 2.60 A; A/B=1-144.
DR PDB; 3VOD; X-ray; 2.60 A; A/B=1-144.
DR PDB; 3VOE; X-ray; 2.60 A; A/B=1-144.
DR PDB; 4JBA; X-ray; 2.50 A; A/B=1-144.
DR PDB; 5H3R; X-ray; 2.67 A; A/B=1-144.
DR PDBsum; 1JGS; -.
DR PDBsum; 3VB2; -.
DR PDBsum; 3VOD; -.
DR PDBsum; 3VOE; -.
DR PDBsum; 4JBA; -.
DR PDBsum; 5H3R; -.
DR AlphaFoldDB; P27245; -.
DR SMR; P27245; -.
DR BioGRID; 4259660; 138.
DR DIP; DIP-10164N; -.
DR STRING; 511145.b1530; -.
DR jPOST; P27245; -.
DR PaxDb; P27245; -.
DR PRIDE; P27245; -.
DR EnsemblBacteria; AAC74603; AAC74603; b1530.
DR EnsemblBacteria; BAA15220; BAA15220; BAA15220.
DR GeneID; 945825; -.
DR KEGG; ecj:JW5248; -.
DR KEGG; eco:b1530; -.
DR PATRIC; fig|1411691.4.peg.736; -.
DR EchoBASE; EB1405; -.
DR eggNOG; COG1846; Bacteria.
DR HOGENOM; CLU_083287_18_5_6; -.
DR InParanoid; P27245; -.
DR OMA; YEATMVT; -.
DR PhylomeDB; P27245; -.
DR BioCyc; EcoCyc:PD00364; -.
DR EvolutionaryTrace; P27245; -.
DR PRO; PR:P27245; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0071236; P:cellular response to antibiotic; IMP:EcoCyc.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:EcoCyc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IMP:EcoCyc.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000835; HTH_MarR-typ.
DR InterPro; IPR023187; Tscrpt_reg_MarR-type_CS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF01047; MarR; 1.
DR PRINTS; PR00598; HTHMARR.
DR SMART; SM00347; HTH_MARR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS01117; HTH_MARR_1; 1.
DR PROSITE; PS50995; HTH_MARR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; DNA-binding; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..144
FT /note="Multiple antibiotic resistance protein MarR"
FT /id="PRO_0000054362"
FT DOMAIN 11..144
FT /note="HTH marR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00345"
FT MUTAGEN 45
FT /note="V->E: Increased transcription of the region II
FT transcript."
FT /evidence="ECO:0000269|PubMed:10760140"
FT MUTAGEN 77
FT /note="R->L: Increased transcription of the region II
FT transcript."
FT /evidence="ECO:0000269|PubMed:10760140"
FT MUTAGEN 123..144
FT /note="Missing: Increased transcription of the region II
FT transcript."
FT /evidence="ECO:0000269|PubMed:10760140"
FT HELIX 7..11
FT /evidence="ECO:0007829|PDB:5H3R"
FT HELIX 14..33
FT /evidence="ECO:0007829|PDB:1JGS"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:1JGS"
FT HELIX 40..52
FT /evidence="ECO:0007829|PDB:1JGS"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1JGS"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:1JGS"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:1JGS"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:1JGS"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:3VOD"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:1JGS"
FT HELIX 102..124
FT /evidence="ECO:0007829|PDB:1JGS"
FT TURN 125..130
FT /evidence="ECO:0007829|PDB:1JGS"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:1JGS"
SQ SEQUENCE 144 AA; 16065 MW; BE7DF5549E24D1D3 CRC64;
MKSTSDLFNE IIPLGRLIHM VNQKKDRLLN EYLSPLDITA AQFKVLCSIR CAACITPVEL
KKVLSVDLGA LTRMLDRLVC KGWVERLPNP NDKRGVLVKL TTGGAAICEQ CHQLVGQDLH
QELTKNLTAD EVATLEYLLK KVLP
