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Multidrug transporter MdfA (Chloramphenicol resistance pump Cmr)

 MDFA_ECOLI              Reviewed;         410 AA.
P0AEY8; P71226; P75807; Q46966;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 1.
25-OCT-2017, entry version 99.
RecName: Full=Multidrug transporter MdfA;
AltName: Full=Chloramphenicol resistance pump Cmr;
Name=mdfA; Synonyms=cmlA, cmr; OrderedLocusNames=b0842, JW0826;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=8655497; DOI=10.1128/jb.178.11.3188-3193.1996;
Nilsen I.W., Bakke I., Vader A., Olsvik O., El-Gewely M.R.;
"Isolation of cmr, a novel Escherichia coli chloramphenicol resistance
gene encoding a putative efflux pump.";
J. Bacteriol. 178:3188-3193(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=ATCC 33694 / HB101;
PubMed=9079913; DOI=10.1128/jb.179.7.2274-2280.1997;
Edgar R., Bibi E.;
"MdfA, an Escherichia coli multidrug resistance protein with an
extraordinarily broad spectrum of drug recognition.";
J. Bacteriol. 179:2274-2280(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
FUNCTION.
STRAIN=K12 / C600 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
PubMed=9811673;
Bohn C., Bouloc P.;
"The Escherichia coli cmlA gene encodes the multidrug efflux pump
Cmr/MdfA and is responsible for isopropyl-beta-D-thiogalactopyranoside
exclusion and spectinomycin sensitivity.";
J. Bacteriol. 180:6072-6075(1998).
[7]
FUNCTION AS AN ANTIPORTER, ENZYME REGULATION, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=9644262; DOI=10.1093/oxfordjournals.jbchem.a022078;
Mine T., Morita Y., Kataoka A., Mizushima T., Tsuchiya T.;
"Evidence for chloramphenicol/H+ antiport in Cmr (MdfA) system of
Escherichia coli and properties of the antiporter.";
J. Biochem. 124:187-193(1998).
[8]
TOPOLOGY.
PubMed=10022825; DOI=10.1093/emboj/18.4.822;
Edgar R., Bibi E.;
"A single membrane-embedded negative charge is critical for
recognizing positively charged drugs by the Escherichia coli multidrug
resistance protein MdfA.";
EMBO J. 18:822-832(1999).
[9]
FUNCTION.
PubMed=12578981; DOI=10.1073/pnas.0435544100;
Lewinson O., Adler J., Poelarends G.J., Mazurkiewicz P.,
Driessen A.J., Bibi E.;
"The Escherichia coli multidrug transporter MdfA catalyzes both
electrogenic and electroneutral transport reactions.";
Proc. Natl. Acad. Sci. U.S.A. 100:1667-1672(2003).
[10]
MUTAGENESIS OF GLU-26.
PubMed=14717607; DOI=10.1021/bi035485t;
Adler J., Lewinson O., Bibi E.;
"Role of a conserved membrane-embedded acidic residue in the multidrug
transporter MdfA.";
Biochemistry 43:518-525(2004).
[11]
FUNCTION IN ALKALITOLERANCE.
PubMed=15371593; DOI=10.1073/pnas.0405375101;
Lewinson O., Padan E., Bibi E.;
"Alkalitolerance: a biological function for a multidrug transporter in
pH homeostasis.";
Proc. Natl. Acad. Sci. U.S.A. 101:14073-14078(2004).
[12]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15919996; DOI=10.1126/science.1109730;
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane
proteome.";
Science 308:1321-1323(2005).
[13]
SUBUNIT.
PubMed=17407265; DOI=10.1021/bi602405w;
Sigal N., Lewinson O., Wolf S.G., Bibi E.;
"E. coli multidrug transporter MdfA is a monomer.";
Biochemistry 46:5200-5208(2007).
[14]
SUBSTRATE-BINDING.
PubMed=19808670; DOI=10.1074/jbc.M109.050658;
Fluman N., Cohen-Karni D., Weiss T., Bibi E.;
"A promiscuous conformational switch in the secondary multidrug
transporter MdfA.";
J. Biol. Chem. 284:32296-32304(2009).
-!- FUNCTION: 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(+).
{ECO:0000269|PubMed:12578981, ECO:0000269|PubMed:15371593,
ECO:0000269|PubMed:9079913, ECO:0000269|PubMed:9644262,
ECO:0000269|PubMed:9811673}.
-!- ENZYME REGULATION: Inhibited by CCCP.
{ECO:0000269|PubMed:9644262}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 6.5. {ECO:0000269|PubMed:9644262};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17407265}.
-!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
protein.
-!- 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.
-!- MISCELLANEOUS: 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.
-!- SIMILARITY: Belongs to the major facilitator superfamily. MdfA
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U44900; AAC44147.1; -; Genomic_DNA.
EMBL; Y08743; CAA69997.1; -; Genomic_DNA.
EMBL; U00096; AAC73929.1; -; Genomic_DNA.
EMBL; AP009048; BAA35546.1; -; Genomic_DNA.
PIR; B64822; B64822.
RefSeq; NP_415363.1; NC_000913.3.
RefSeq; WP_001180089.1; NZ_LN832404.1.
PDB; 4ZOW; X-ray; 2.45 A; A=10-400.
PDB; 4ZP0; X-ray; 2.00 A; A=9-400.
PDB; 4ZP2; X-ray; 2.20 A; A=9-400.
PDBsum; 4ZOW; -.
PDBsum; 4ZP0; -.
PDBsum; 4ZP2; -.
ProteinModelPortal; P0AEY8; -.
SMR; P0AEY8; -.
BioGrid; 4262828; 106.
DIP; DIP-48116N; -.
IntAct; P0AEY8; 1.
MINT; MINT-1227586; -.
STRING; 316385.ECDH10B_0911; -.
BindingDB; P0AEY8; -.
ChEMBL; CHEMBL4785; -.
TCDB; 2.A.1.2.19; the major facilitator superfamily (mfs).
PaxDb; P0AEY8; -.
PRIDE; P0AEY8; -.
EnsemblBacteria; AAC73929; AAC73929; b0842.
EnsemblBacteria; BAA35546; BAA35546; BAA35546.
GeneID; 945448; -.
KEGG; ag:CAA69997; -.
KEGG; ecj:JW0826; -.
KEGG; eco:b0842; -.
PATRIC; fig|1411691.4.peg.1436; -.
EchoBASE; EB3460; -.
EcoGene; EG13696; mdfA.
eggNOG; ENOG4107QF7; Bacteria.
eggNOG; ENOG410XT98; LUCA.
HOGENOM; HOG000118215; -.
InParanoid; P0AEY8; -.
KO; K08160; -.
PhylomeDB; P0AEY8; -.
BioCyc; EcoCyc:CMR-MONOMER; -.
BioCyc; MetaCyc:CMR-MONOMER; -.
PRO; PR:P0AEY8; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
GO; GO:0015238; F:drug transmembrane transporter activity; IMP:EcoCyc.
GO; GO:0015386; F:potassium:proton antiporter activity; IDA:EcoCyc.
GO; GO:0015385; F:sodium:proton antiporter activity; IDA:EcoCyc.
GO; GO:0006855; P:drug transmembrane transport; IMP:EcoCyc.
GO; GO:0030641; P:regulation of cellular pH; IMP:EcoCyc.
GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
CDD; cd06174; MFS; 1.
InterPro; IPR011701; MFS.
InterPro; IPR020846; MFS_dom.
InterPro; IPR036259; MFS_trans_sf.
InterPro; IPR005829; Sugar_transporter_CS.
Pfam; PF07690; MFS_1; 1.
SUPFAM; SSF103473; SSF103473; 1.
PROSITE; PS50850; MFS; 1.
1: Evidence at protein level;
3D-structure; Antibiotic resistance; Cell inner membrane;
Cell membrane; Complete proteome; Membrane; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 410 Multidrug transporter MdfA.
/FTId=PRO_0000173331.
TOPO_DOM 1 14 Cytoplasmic. {ECO:0000305}.
TRANSMEM 15 32 Helical. {ECO:0000305}.
TOPO_DOM 33 53 Periplasmic. {ECO:0000305}.
TRANSMEM 54 72 Helical. {ECO:0000305}.
TOPO_DOM 73 82 Cytoplasmic. {ECO:0000305}.
TRANSMEM 83 103 Helical. {ECO:0000305}.
TOPO_DOM 104 109 Periplasmic. {ECO:0000305}.
TRANSMEM 110 130 Helical. {ECO:0000305}.
TOPO_DOM 131 144 Cytoplasmic. {ECO:0000305}.
TRANSMEM 145 165 Helical. {ECO:0000305}.
TOPO_DOM 166 166 Periplasmic. {ECO:0000305}.
TRANSMEM 167 187 Helical. {ECO:0000305}.
TOPO_DOM 188 226 Cytoplasmic. {ECO:0000305}.
TRANSMEM 227 247 Helical. {ECO:0000305}.
TOPO_DOM 248 255 Periplasmic. {ECO:0000305}.
TRANSMEM 256 276 Helical. {ECO:0000305}.
TOPO_DOM 277 287 Cytoplasmic. {ECO:0000305}.
TRANSMEM 288 308 Helical. {ECO:0000305}.
TOPO_DOM 309 314 Periplasmic. {ECO:0000305}.
TRANSMEM 315 335 Helical. {ECO:0000305}.
TOPO_DOM 336 346 Cytoplasmic. {ECO:0000305}.
TRANSMEM 347 367 Helical. {ECO:0000305}.
TOPO_DOM 368 378 Periplasmic. {ECO:0000305}.
TRANSMEM 379 399 Helical. {ECO:0000305}.
TOPO_DOM 400 410 Cytoplasmic. {ECO:0000305}.
MUTAGEN 26 26 E->A: Loss of ethidium bromide efflux
activity. {ECO:0000269|PubMed:14717607}.
MUTAGEN 26 26 E->D: No change in ethidium bromide
efflux activity.
{ECO:0000269|PubMed:14717607}.
MUTAGEN 26 26 E->H: Almost no chloramphenicol efflux
activity. Loss of ethidium bromide efflux
activity. {ECO:0000269|PubMed:14717607}.
MUTAGEN 26 26 E->I,V: Slight decrease in
chloramphenicol efflux activity. Exhibits
low ethidium bromide efflux activity.
{ECO:0000269|PubMed:14717607}.
MUTAGEN 26 26 E->K: Decrease in TPP efflux activity.
Exhibits low ethidium bromide efflux
activity. {ECO:0000269|PubMed:14717607}.
MUTAGEN 26 26 E->L,N: Strong decrease in
chloramphenicol efflux activity. Loss of
ethidium bromide and TPP efflux
activities.
{ECO:0000269|PubMed:14717607}.
MUTAGEN 26 26 E->Q: Slight decrease in chloramphenicol
efflux activity. Loss of ethidium bromide
efflux activity.
{ECO:0000269|PubMed:14717607}.
MUTAGEN 26 26 E->T: Strong decrease in chloramphenicol
efflux activity. Loss of ethidium bromide
efflux activity.
{ECO:0000269|PubMed:14717607}.
CONFLICT 59 59 T -> N (in Ref. 2; CAA69997).
{ECO:0000305}.
CONFLICT 225 240 ALALGFVSLPLLAWIA -> GAGAADSLVCRCWRGSP (in
Ref. 1; AAC44147). {ECO:0000305}.
STRAND 11 13 {ECO:0000244|PDB:4ZP2}.
HELIX 14 16 {ECO:0000244|PDB:4ZP2}.
HELIX 17 34 {ECO:0000244|PDB:4ZP0}.
HELIX 36 46 {ECO:0000244|PDB:4ZP0}.
HELIX 53 65 {ECO:0000244|PDB:4ZP0}.
HELIX 69 79 {ECO:0000244|PDB:4ZP0}.
HELIX 81 98 {ECO:0000244|PDB:4ZP0}.
HELIX 99 101 {ECO:0000244|PDB:4ZP0}.
HELIX 105 116 {ECO:0000244|PDB:4ZP0}.
HELIX 117 120 {ECO:0000244|PDB:4ZP0}.
HELIX 121 124 {ECO:0000244|PDB:4ZP0}.
HELIX 126 133 {ECO:0000244|PDB:4ZP0}.
HELIX 136 165 {ECO:0000244|PDB:4ZP0}.
HELIX 170 191 {ECO:0000244|PDB:4ZP0}.
HELIX 205 216 {ECO:0000244|PDB:4ZP0}.
HELIX 219 246 {ECO:0000244|PDB:4ZP0}.
TURN 247 249 {ECO:0000244|PDB:4ZP0}.
HELIX 254 278 {ECO:0000244|PDB:4ZP0}.
HELIX 279 281 {ECO:0000244|PDB:4ZP0}.
HELIX 284 308 {ECO:0000244|PDB:4ZP0}.
HELIX 313 339 {ECO:0000244|PDB:4ZP0}.
HELIX 346 398 {ECO:0000244|PDB:4ZP0}.
SEQUENCE 410 AA; 44321 MW; D4466EE680095773 CRC64;
MQNKLASGAR LGRQALLFPL CLVLYEFSTY IGNDMIQPGM LAVVEQYQAG IDWVPTSMTA
YLAGGMFLQW LLGPLSDRIG RRPVMLAGVV WFIVTCLAIL LAQNIEQFTL LRFLQGISLC
FIGAVGYAAI QESFEEAVCI KITALMANVA LIAPLLGPLV GAAWIHVLPW EGMFVLFAAL
AAISFFGLQR AMPETATRIG EKLSLKELGR DYKLVLKNGR FVAGALALGF VSLPLLAWIA
QSPIIIITGE QLSSYEYGLL QVPIFGALIA GNLLLARLTS RRTVRSLIIM GGWPIMIGLL
VAAAATVISS HAYLWMTAGL SIYAFGIGLA NAGLVRLTLF ASDMSKGTVS AAMGMLQMLI
FTVGIEISKH AWLNGGNGLF NLFNLVNGIL WLSLMVIFLK DKQMGNSHEG


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