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Protein

Multiple antibiotic resistance protein MarR

Gene

marR

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Repressor of the marRAB operon which is involved in the activation of both antibiotic resistance and oxidative stress genes. Binds to the marO operator/promoter site.

GO - Molecular functioni

  • DNA binding Source: EcoCyc
  • sequence-specific DNA binding transcription factor activity Source: InterPro

GO - Biological processi

  • cellular response to antibiotic Source: EcoCyc
  • negative regulation of transcription, DNA-templated Source: EcoCyc
  • response to heat Source: EcoCyc
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Antibiotic resistance, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:PD00364.
ECOL316407:JW5248-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Multiple antibiotic resistance protein MarR
Gene namesi
Name:marR
Synonyms:cfxB, inaR, soxQ
Ordered Locus Names:b1530, JW5248
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11435. marR.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi45 – 451V → E: Increased transcription of the region II transcript. 1 Publication
Mutagenesisi77 – 771R → L: Increased transcription of the region II transcript. 1 Publication
Mutagenesisi123 – 14422Missing : Increased transcription of the region II transcript. 1 PublicationAdd
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 144144Multiple antibiotic resistance protein MarRPRO_0000054362Add
BLAST

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
gyrAP0AES42EBI-6409744,EBI-547129

Protein-protein interaction databases

DIPiDIP-10164N.
IntActiP27245. 1 interaction.
STRINGi511145.b1530.

Structurei

Secondary structure

1
144
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 3320Combined sources
Turni34 – 374Combined sources
Helixi40 – 5213Combined sources
Beta strandi53 – 553Combined sources
Helixi57 – 648Combined sources
Helixi68 – 8013Combined sources
Beta strandi83 – 886Combined sources
Turni90 – 923Combined sources
Beta strandi96 – 1005Combined sources
Helixi102 – 12423Combined sources
Turni125 – 1306Combined sources
Helixi132 – 1409Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JGSX-ray2.30A7-144[»]
3VB2X-ray2.60A/B1-144[»]
3VODX-ray2.60A/B1-144[»]
3VOEX-ray2.60A/B1-144[»]
4JBAX-ray2.50A/B1-144[»]
ProteinModelPortaliP27245.
SMRiP27245. Positions 7-144.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27245.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 144134HTH marR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HTH marR-type DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1846.
HOGENOMiHOG000221449.
InParanoidiP27245.
KOiK03712.
OMAiDHITLTR.
OrthoDBiEOG6PGKBH.
PhylomeDBiP27245.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR000835. HTH_MarR-typ.
IPR023187. Tscrpt_reg_MarR-type_CS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01047. MarR. 1 hit.
[Graphical view]
PRINTSiPR00598. HTHMARR.
SMARTiSM00347. HTH_MARR. 1 hit.
[Graphical view]
PROSITEiPS01117. HTH_MARR_1. 1 hit.
PS50995. HTH_MARR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P27245-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSTSDLFNE IIPLGRLIHM VNQKKDRLLN EYLSPLDITA AQFKVLCSIR
60 70 80 90 100
CAACITPVEL KKVLSVDLGA LTRMLDRLVC KGWVERLPNP NDKRGVLVKL
110 120 130 140
TTGGAAICEQ CHQLVGQDLH QELTKNLTAD EVATLEYLLK KVLP
Length:144
Mass (Da):16,065
Last modified:December 1, 2000 - v2
Checksum:iBE7DF5549E24D1D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96235 Genomic DNA. Translation: AAC16394.2.
U00096 Genomic DNA. Translation: AAC74603.2.
AP009048 Genomic DNA. Translation: BAA15220.1.
PIRiE64907.
RefSeqiNP_416047.4. NC_000913.3.
WP_000843414.1. NZ_CP010445.1.

Genome annotation databases

EnsemblBacteriaiAAC74603; AAC74603; b1530.
BAA15220; BAA15220; BAA15220.
GeneIDi945825.
KEGGieco:b1530.
PATRICi32118358. VBIEscCol129921_1599.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96235 Genomic DNA. Translation: AAC16394.2.
U00096 Genomic DNA. Translation: AAC74603.2.
AP009048 Genomic DNA. Translation: BAA15220.1.
PIRiE64907.
RefSeqiNP_416047.4. NC_000913.3.
WP_000843414.1. NZ_CP010445.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JGSX-ray2.30A7-144[»]
3VB2X-ray2.60A/B1-144[»]
3VODX-ray2.60A/B1-144[»]
3VOEX-ray2.60A/B1-144[»]
4JBAX-ray2.50A/B1-144[»]
ProteinModelPortaliP27245.
SMRiP27245. Positions 7-144.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10164N.
IntActiP27245. 1 interaction.
STRINGi511145.b1530.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74603; AAC74603; b1530.
BAA15220; BAA15220; BAA15220.
GeneIDi945825.
KEGGieco:b1530.
PATRICi32118358. VBIEscCol129921_1599.

Organism-specific databases

EchoBASEiEB1405.
EcoGeneiEG11435. marR.

Phylogenomic databases

eggNOGiCOG1846.
HOGENOMiHOG000221449.
InParanoidiP27245.
KOiK03712.
OMAiDHITLTR.
OrthoDBiEOG6PGKBH.
PhylomeDBiP27245.

Enzyme and pathway databases

BioCyciEcoCyc:PD00364.
ECOL316407:JW5248-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP27245.
PROiP27245.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR000835. HTH_MarR-typ.
IPR023187. Tscrpt_reg_MarR-type_CS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01047. MarR. 1 hit.
[Graphical view]
PRINTSiPR00598. HTHMARR.
SMARTiSM00347. HTH_MARR. 1 hit.
[Graphical view]
PROSITEiPS01117. HTH_MARR_1. 1 hit.
PS50995. HTH_MARR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genetic and functional analysis of the multiple antibiotic resistance (mar) locus in Escherichia coli."
    Cohen S.P., Haechler H., Levy S.B.
    J. Bacteriol. 175:1484-1492(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Repressor mutations in the marRAB operon that activate oxidative stress genes and multiple antibiotic resistance in Escherichia coli."
    Ariza R.R., Cohen S.P., Bachhawat N., Levy S.B., Demple B.
    J. Bacteriol. 176:143-148(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "Characterization of MarR, the repressor of the multiple antibiotic resistance (mar) operon in Escherichia coli."
    Seoane A.S., Levy S.B.
    J. Bacteriol. 177:3414-3419(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "Mutational analysis of MarR, the negative regulator of marRAB expression in Escherichia coli, suggests the presence of two regions required for DNA binding."
    Alekshun M.N., Kim Y.S., Levy S.B.
    Mol. Microbiol. 35:1394-1404(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.

Entry informationi

Entry nameiMARR_ECOLI
AccessioniPrimary (citable) accession number: P27245
Secondary accession number(s): P76882, P77582
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: December 1, 2000
Last modified: July 22, 2015
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.