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Protein

Multidrug transporter MdfA

Gene

mdfA

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

Functioni

Efflux pump driven by the proton motive force. Confers resistance to a broad spectrum of chemically unrelated drugs. Confers resistance to a diverse group of cationic or zwitterionic lipophilic compounds such as ethidium bromide, tetraphenylphosphonium, rhodamine, daunomycin, benzalkonium, rifampicin, tetracycline, puromycin, and to chemically unrelated, clinically important antibiotics such as chloramphenicol, erythromycin, and certain aminoglycosides and fluoroquinolones. Overexpression results in isopropyl-beta-D-thiogalactopyranoside (IPTG) exclusion and spectinomycin sensitivity. Transport of neutral substrates is electrogenic, whereas transport of cationic substrates is electroneutral. In addition to its role in multidrug resistance, confers extreme alkaline pH resistance, allowing the growth under conditions that are close to those used normally by alkaliphiles. This activity requires Na+ or K+.5 Publications

Enzyme regulationi

Inhibited by CCCP.1 Publication

pH dependencei

Optimum pH is 6.5.1 Publication

GO - Molecular functioni

  • drug transmembrane transporter activity Source: EcoCyc
  • potassium:proton antiporter activity Source: EcoCyc
  • sodium:proton antiporter activity Source: EcoCyc

GO - Biological processi

  • drug transmembrane transport Source: EcoCyc
  • regulation of cellular pH Source: EcoCyc
  • response to antibiotic Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Antibiotic resistance, Transport

Enzyme and pathway databases

BioCyciEcoCyc:CMR-MONOMER.
ECOL316407:JW0826-MONOMER.
MetaCyc:CMR-MONOMER.

Protein family/group databases

TCDBi2.A.1.2.19. the major facilitator superfamily (mfs).

Names & Taxonomyi

Protein namesi
Recommended name:
Multidrug transporter MdfA
Alternative name(s):
Chloramphenicol resistance pump Cmr
Gene namesi
Name:mdfA
Synonyms:cmlA, cmr
Ordered Locus Names:b0842, JW0826
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13696. mdfA.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 14CytoplasmicCuratedAdd BLAST14
Transmembranei15 – 32HelicalCuratedAdd BLAST18
Topological domaini33 – 53PeriplasmicCuratedAdd BLAST21
Transmembranei54 – 72HelicalCuratedAdd BLAST19
Topological domaini73 – 82CytoplasmicCurated10
Transmembranei83 – 103HelicalCuratedAdd BLAST21
Topological domaini104 – 109PeriplasmicCurated6
Transmembranei110 – 130HelicalCuratedAdd BLAST21
Topological domaini131 – 144CytoplasmicCuratedAdd BLAST14
Transmembranei145 – 165HelicalCuratedAdd BLAST21
Topological domaini166PeriplasmicCurated1
Transmembranei167 – 187HelicalCuratedAdd BLAST21
Topological domaini188 – 226CytoplasmicCuratedAdd BLAST39
Transmembranei227 – 247HelicalCuratedAdd BLAST21
Topological domaini248 – 255PeriplasmicCurated8
Transmembranei256 – 276HelicalCuratedAdd BLAST21
Topological domaini277 – 287CytoplasmicCuratedAdd BLAST11
Transmembranei288 – 308HelicalCuratedAdd BLAST21
Topological domaini309 – 314PeriplasmicCurated6
Transmembranei315 – 335HelicalCuratedAdd BLAST21
Topological domaini336 – 346CytoplasmicCuratedAdd BLAST11
Transmembranei347 – 367HelicalCuratedAdd BLAST21
Topological domaini368 – 378PeriplasmicCuratedAdd BLAST11
Transmembranei379 – 399HelicalCuratedAdd BLAST21
Topological domaini400 – 410CytoplasmicCuratedAdd BLAST11

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi26E → A: Loss of ethidium bromide efflux activity. 1 Publication1
Mutagenesisi26E → D: No change in ethidium bromide efflux activity. 1 Publication1
Mutagenesisi26E → H: Almost no chloramphenicol efflux activity. Loss of ethidium bromide efflux activity. 1 Publication1
Mutagenesisi26E → I or V: Slight decrease in chloramphenicol efflux activity. Exhibits low ethidium bromide efflux activity. 1 Publication1
Mutagenesisi26E → K: Decrease in TPP efflux activity. Exhibits low ethidium bromide efflux activity. 1 Publication1
Mutagenesisi26E → L or N: Strong decrease in chloramphenicol efflux activity. Loss of ethidium bromide and TPP efflux activities. 1 Publication1
Mutagenesisi26E → Q: Slight decrease in chloramphenicol efflux activity. Loss of ethidium bromide efflux activity. 1 Publication1
Mutagenesisi26E → T: Strong decrease in chloramphenicol efflux activity. Loss of ethidium bromide efflux activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL4785.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001733311 – 410Multidrug transporter MdfAAdd BLAST410

Proteomic databases

PaxDbiP0AEY8.
PRIDEiP0AEY8.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi4262828. 106 interactors.
DIPiDIP-48116N.
IntActiP0AEY8. 1 interactor.
MINTiMINT-1227586.
STRINGi511145.b0842.

Chemistry databases

BindingDBiP0AEY8.

Structurei

Secondary structure

1410
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 13Combined sources3
Helixi14 – 16Combined sources3
Helixi17 – 34Combined sources18
Helixi36 – 46Combined sources11
Helixi53 – 65Combined sources13
Helixi69 – 79Combined sources11
Helixi81 – 98Combined sources18
Helixi99 – 101Combined sources3
Helixi105 – 116Combined sources12
Helixi117 – 120Combined sources4
Helixi121 – 124Combined sources4
Helixi126 – 133Combined sources8
Helixi136 – 165Combined sources30
Helixi170 – 191Combined sources22
Helixi205 – 216Combined sources12
Helixi219 – 246Combined sources28
Turni247 – 249Combined sources3
Helixi254 – 278Combined sources25
Helixi279 – 281Combined sources3
Helixi284 – 308Combined sources25
Helixi313 – 339Combined sources27
Helixi346 – 398Combined sources53

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZOWX-ray2.45A10-400[»]
4ZP0X-ray2.00A9-400[»]
4ZP2X-ray2.20A9-400[»]
ProteinModelPortaliP0AEY8.
SMRiP0AEY8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4107QF7. Bacteria.
ENOG410XT98. LUCA.
HOGENOMiHOG000118215.
InParanoidiP0AEY8.
KOiK08160.
OMAiMQTHANR.
PhylomeDBiP0AEY8.

Family and domain databases

CDDicd06174. MFS. 1 hit.
InterProiIPR011701. MFS.
IPR020846. MFS_dom.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamiPF07690. MFS_1. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AEY8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQNKLASGAR LGRQALLFPL CLVLYEFSTY IGNDMIQPGM LAVVEQYQAG
60 70 80 90 100
IDWVPTSMTA YLAGGMFLQW LLGPLSDRIG RRPVMLAGVV WFIVTCLAIL
110 120 130 140 150
LAQNIEQFTL LRFLQGISLC FIGAVGYAAI QESFEEAVCI KITALMANVA
160 170 180 190 200
LIAPLLGPLV GAAWIHVLPW EGMFVLFAAL AAISFFGLQR AMPETATRIG
210 220 230 240 250
EKLSLKELGR DYKLVLKNGR FVAGALALGF VSLPLLAWIA QSPIIIITGE
260 270 280 290 300
QLSSYEYGLL QVPIFGALIA GNLLLARLTS RRTVRSLIIM GGWPIMIGLL
310 320 330 340 350
VAAAATVISS HAYLWMTAGL SIYAFGIGLA NAGLVRLTLF ASDMSKGTVS
360 370 380 390 400
AAMGMLQMLI FTVGIEISKH AWLNGGNGLF NLFNLVNGIL WLSLMVIFLK
410
DKQMGNSHEG
Length:410
Mass (Da):44,321
Last modified:December 20, 2005 - v1
Checksum:iD4466EE680095773
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti59T → N in CAA69997 (PubMed:9079913).Curated1
Sequence conflicti225 – 240ALALG…LAWIA → GAGAADSLVCRCWRGSP in AAC44147 (PubMed:8655497).CuratedAdd BLAST16

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U44900 Genomic DNA. Translation: AAC44147.1.
Y08743 Genomic DNA. Translation: CAA69997.1.
U00096 Genomic DNA. Translation: AAC73929.1.
AP009048 Genomic DNA. Translation: BAA35546.1.
PIRiB64822.
RefSeqiNP_415363.1. NC_000913.3.
WP_001180089.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73929; AAC73929; b0842.
BAA35546; BAA35546; BAA35546.
GeneIDi945448.
KEGGiag:CAA69997.
ecj:JW0826.
eco:b0842.
PATRICi32116889. VBIEscCol129921_0870.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U44900 Genomic DNA. Translation: AAC44147.1.
Y08743 Genomic DNA. Translation: CAA69997.1.
U00096 Genomic DNA. Translation: AAC73929.1.
AP009048 Genomic DNA. Translation: BAA35546.1.
PIRiB64822.
RefSeqiNP_415363.1. NC_000913.3.
WP_001180089.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4ZOWX-ray2.45A10-400[»]
4ZP0X-ray2.00A9-400[»]
4ZP2X-ray2.20A9-400[»]
ProteinModelPortaliP0AEY8.
SMRiP0AEY8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262828. 106 interactors.
DIPiDIP-48116N.
IntActiP0AEY8. 1 interactor.
MINTiMINT-1227586.
STRINGi511145.b0842.

Chemistry databases

BindingDBiP0AEY8.
ChEMBLiCHEMBL4785.

Protein family/group databases

TCDBi2.A.1.2.19. the major facilitator superfamily (mfs).

Proteomic databases

PaxDbiP0AEY8.
PRIDEiP0AEY8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73929; AAC73929; b0842.
BAA35546; BAA35546; BAA35546.
GeneIDi945448.
KEGGiag:CAA69997.
ecj:JW0826.
eco:b0842.
PATRICi32116889. VBIEscCol129921_0870.

Organism-specific databases

EchoBASEiEB3460.
EcoGeneiEG13696. mdfA.

Phylogenomic databases

eggNOGiENOG4107QF7. Bacteria.
ENOG410XT98. LUCA.
HOGENOMiHOG000118215.
InParanoidiP0AEY8.
KOiK08160.
OMAiMQTHANR.
PhylomeDBiP0AEY8.

Enzyme and pathway databases

BioCyciEcoCyc:CMR-MONOMER.
ECOL316407:JW0826-MONOMER.
MetaCyc:CMR-MONOMER.

Miscellaneous databases

PROiP0AEY8.

Family and domain databases

CDDicd06174. MFS. 1 hit.
InterProiIPR011701. MFS.
IPR020846. MFS_dom.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamiPF07690. MFS_1. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMDFA_ECOLI
AccessioniPrimary (citable) accession number: P0AEY8
Secondary accession number(s): P71226, P75807, Q46966
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: November 2, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

A negative charge at position 26 is required for efficient transport of positively charged substrates, but not for neutral compounds. This negative charge does not play an essential role in the multidrug transport mechanism.
Has a sensitive conformational switch that can be triggered either by substrate binding or by attaching unrelated agents inside the pocket. Dissimilar substrates induce similar conformational changes.

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

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 one 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.