EMRD_ECOLI
ID EMRD_ECOLI Reviewed; 394 AA.
AC P31442; Q2M7Y6;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Multidrug resistance protein D;
GN Name=emrD; Synonyms=yicQ; OrderedLocusNames=b3673, JW5634;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=8240355; DOI=10.1006/bbrc.1993.2320;
RA Naroditskaya V., Schloseer M.J., Fan N.Y., Lewis K.;
RT "An E. coli gene emrD is involved in adaptation to low energy shock.";
RL Biochem. Biophys. Res. Commun. 196:803-809(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
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 TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Multidrug resistance pump that participates in a low energy
CC shock adaptive response.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA62025.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L10328; AAA62025.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76696.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77620.1; -; Genomic_DNA.
DR PIR; B65169; B65169.
DR RefSeq; NP_418129.2; NC_000913.3.
DR RefSeq; WP_000828746.1; NZ_SSZK01000035.1.
DR PDB; 2GFP; X-ray; 3.50 A; A/B=9-383.
DR PDBsum; 2GFP; -.
DR AlphaFoldDB; P31442; -.
DR SMR; P31442; -.
DR BioGRID; 4261242; 128.
DR STRING; 511145.b3673; -.
DR TCDB; 2.A.1.2.9; the major facilitator superfamily (mfs).
DR PaxDb; P31442; -.
DR PRIDE; P31442; -.
DR EnsemblBacteria; AAC76696; AAC76696; b3673.
DR EnsemblBacteria; BAE77620; BAE77620; BAE77620.
DR GeneID; 66672429; -.
DR GeneID; 948180; -.
DR KEGG; ecj:JW5634; -.
DR KEGG; eco:b3673; -.
DR PATRIC; fig|511145.12.peg.3794; -.
DR EchoBASE; EB1644; -.
DR eggNOG; COG2814; Bacteria.
DR HOGENOM; CLU_001265_47_1_6; -.
DR InParanoid; P31442; -.
DR OMA; YYVIVTM; -.
DR PhylomeDB; P31442; -.
DR BioCyc; EcoCyc:EMRD-MON; -.
DR BioCyc; MetaCyc:EMRD-MON; -.
DR EvolutionaryTrace; P31442; -.
DR PRO; PR:P31442; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IMP:EcoCyc.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004734; Multidrug-R.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00880; 2_A_01_02; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..394
FT /note="Multidrug resistance protein D"
FT /id="PRO_0000173326"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..46
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..162
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..242
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..364
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT HELIX 10..35
FT /evidence="ECO:0007829|PDB:2GFP"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:2GFP"
FT HELIX 43..60
FT /evidence="ECO:0007829|PDB:2GFP"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:2GFP"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:2GFP"
FT HELIX 77..126
FT /evidence="ECO:0007829|PDB:2GFP"
FT HELIX 133..154
FT /evidence="ECO:0007829|PDB:2GFP"
FT HELIX 158..176
FT /evidence="ECO:0007829|PDB:2GFP"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:2GFP"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:2GFP"
FT HELIX 202..229
FT /evidence="ECO:0007829|PDB:2GFP"
FT HELIX 235..250
FT /evidence="ECO:0007829|PDB:2GFP"
FT HELIX 252..264
FT /evidence="ECO:0007829|PDB:2GFP"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:2GFP"
FT HELIX 269..283
FT /evidence="ECO:0007829|PDB:2GFP"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:2GFP"
FT HELIX 290..315
FT /evidence="ECO:0007829|PDB:2GFP"
FT HELIX 321..325
FT /evidence="ECO:0007829|PDB:2GFP"
FT HELIX 327..348
FT /evidence="ECO:0007829|PDB:2GFP"
FT HELIX 356..377
FT /evidence="ECO:0007829|PDB:2GFP"
SQ SEQUENCE 394 AA; 42216 MW; 342339DC7265A30B CRC64;
MKRQRNVNLL LMLVLLVAVG QMAQTIYIPA IADMARDLNV REGAVQSVMG AYLLTYGVSQ
LFYGPISDRV GRRPVILVGM SIFMLATLVA VTTSSLTVLI AASAMQGMGT GVGGVMARTL
PRDLYERTQL RHANSLLNMG ILVSPLLAPL IGGLLDTMWN WRACYLFLLV LCAGVTFSMA
RWMPETRPVD APRTRLLTSY KTLFGNSGFN CYLLMLIGGL AGIAAFEACS GVLMGAVLGL
SSMTVSILFI LPIPAAFFGA WFAGRPNKRF STLMWQSVIC CLLAGLLMWI PDWFGVMNVW
TLLVPAALFF FGAGMLFPLA TSGAMEPFPF LAGTAGALVG GLQNIGSGVL ASLSAMLPQT
GQGSLGLLMT LMGLLIVLCW LPLATRMSHQ GQPV
