Multiple antibiotic resistance protein MarR - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (?) or add your own

P27245 (MARR_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 107. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Multiple antibiotic resistance protein MarR

Gene names

Name:	marR
Synonyms:	cfxB, inaR, soxQ
Ordered Locus Names:	b1530, JW5248

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	144 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Sequence similarities	Contains 1 HTH marR-type DNA-binding domain.

Ontologies

Keywords
Biological process	Antibiotic resistance Transcription Transcription regulation
Ligand	DNA-binding
Molecular function	Repressor
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to antibiotic Inferred from mutant phenotype Ref.1. Source: EcoCyc negative regulation of transcription, DNA-dependent Inferred from mutant phenotype Ref.1. Source: EcoCyc transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	intracellular Inferred from electronic annotation. Source: InterPro protein-DNA complex Inferred from direct assay PubMed 7777530. Source: EcoCyc
Molecular_function	DNA binding Inferred from direct assay PubMed 7777530. Source: EcoCyc sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
gyrA	P0AES4	2	EBI-6409744,EBI-547129

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 144

144

Multiple antibiotic resistance protein MarR

PRO_0000054362

Regions

Domain

11 – 144

134

HTH marR-type

Experimental info

Mutagenesis

V → E: Increased transcription of the region II transcript.

Mutagenesis

R → L: Increased transcription of the region II transcript.

Mutagenesis

123 – 144

Missing: Increased transcription of the region II transcript.

Secondary structure

144

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P27245 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: BE7DF5549E24D1D3
Show »

FASTA

144

16,065

        10         20         30         40         50         60 
MKSTSDLFNE IIPLGRLIHM VNQKKDRLLN EYLSPLDITA AQFKVLCSIR CAACITPVEL 

        70         80         90        100        110        120 
KKVLSVDLGA LTRMLDRLVC KGWVERLPNP NDKRGVLVKL TTGGAAICEQ CHQLVGQDLH 

       130        140 
QELTKNLTAD EVATLEYLLK KVLP

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. Horiuchi T. DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M96235 Genomic DNA. Translation: AAC16394.2.
U00096 Genomic DNA. Translation: AAC74603.2.
AP009048 Genomic DNA. Translation: BAA15220.1.

PIR

E64907.

RefSeq

NP_416047.4. NC_000913.2.
YP_489793.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JGS	X-ray	2.30	A	7-144	[»]
3VB2	X-ray	2.60	A/B	1-144	[»]
3VOD	X-ray	2.60	A/B	1-144	[»]
3VOE	X-ray	2.60	A/B	1-144	[»]

ProteinModelPortal

P27245.

SMR

P27245. Positions 7-144.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10164N.

IntAct

P27245. 1 interaction.

STRING

511145.b1530.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74603; AAC74603; b1530.
BAA15220; BAA15220; BAA15220.

GeneID

12930666.
945825.

KEGG

ecj:Y75_p1505.
eco:b1530.

PATRIC

32118358. VBIEscCol129921_1599.

Organism-specific databases

EchoBASE

EB1405.

EcoGene

EG11435. marR.

Phylogenomic databases

eggNOG

COG1846.

HOGENOM

HOG000221449.

K03712.

OMA

DITASQF.

ProtClustDB

PRK11512.

Enzyme and pathway databases

BioCyc

EcoCyc:PD00364.
ECOL316407:JW5248-MONOMER.

Gene expression databases

Genevestigator

P27245.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.

InterPro

IPR000835. Tscrpt_reg_HTH_MarR-typ.
IPR023187. Tscrpt_reg_MarR-type_CS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

Pfam

PF01047. MarR. 1 hit.
[Graphical view]

PRINTS

PR00598. HTHMARR.

SMART

SM00347. HTH_MARR. 1 hit.
[Graphical view]

PROSITE

PS01117. HTH_MARR_1. 1 hit.
PS50995. HTH_MARR_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P27245.

Entry information

Entry name

MARR_ECOLI

Accession

Primary (citable) accession number: P27245
Secondary accession number(s): P76882, P77582

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents