EMRK_ECOLI
ID EMRK_ECOLI Reviewed; 387 AA.
AC P52599; P76517; P76944; P76945;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Probable multidrug resistance protein EmrK;
GN Name=emrK; OrderedLocusNames=b2368, JW2365;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Utsumi R.;
RT "Analysis and characterization of the upstream region of evgA and evgS.";
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
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 INDUCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12501312; DOI=10.2323/jgam.43.257;
RA Tanabe H., Yamasak K., Furue M., Yamamoto K., Katoh A., Yamamoto M.,
RA Yoshioka S., Tagami H., Aiba H.A., Utsumi R.;
RT "Growth phase-dependent transcription of emrKY, a homolog of multidrug
RT efflux emrAB genes of Escherichia coli, is induced by tetracycline.";
RL J. Gen. Appl. Microbiol. 43:257-263(1997).
RN [6]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=20128927; DOI=10.1186/1471-2180-10-35;
RA Han X., Dorsey-Oresto A., Malik M., Wang J.Y., Drlica K., Zhao X., Lu T.;
RT "Escherichia coli genes that reduce the lethal effects of stress.";
RL BMC Microbiol. 10:35-35(2010).
CC -!- FUNCTION: Part of the tripartite efflux system EmrYK-TolC, which
CC confers resistance to various drugs. {ECO:0000250}.
CC -!- SUBUNIT: Part of the tripartite efflux system EmrYK-TolC, which is
CC composed of an inner membrane transporter, EmrY, a membrane fusion
CC protein, EmrK, and an outer membrane component, TolC. The complex forms
CC a large protein conduit and can translocate molecules across both the
CC inner and outer membranes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}; Periplasmic side {ECO:0000305}.
CC -!- INDUCTION: Growth phase-dependent transcription is induced by
CC tetracycline. Expression may be controlled by both RpoS and the Mar
CC system. {ECO:0000269|PubMed:12501312}.
CC -!- DISRUPTION PHENOTYPE: Mutants are more sensitive to nalidixic acid,
CC mitomycin C and other stresses such as hydrogen peroxide or UV
CC irradiation. {ECO:0000269|PubMed:20128927}.
CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA11236.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D78168; BAA11236.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75427.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16239.2; -; Genomic_DNA.
DR PIR; E65010; E65010.
DR RefSeq; NP_416869.1; NC_000913.3.
DR RefSeq; WP_000435167.1; NZ_SSZK01000006.1.
DR AlphaFoldDB; P52599; -.
DR SMR; P52599; -.
DR BioGRID; 4260557; 148.
DR ComplexPortal; CPX-4273; EmrKY-TolC multidrug efflux transport system.
DR STRING; 511145.b2368; -.
DR PaxDb; P52599; -.
DR PRIDE; P52599; -.
DR EnsemblBacteria; AAC75427; AAC75427; b2368.
DR EnsemblBacteria; BAA16239; BAA16239; BAA16239.
DR GeneID; 946840; -.
DR KEGG; ecj:JW2365; -.
DR KEGG; eco:b2368; -.
DR PATRIC; fig|1411691.4.peg.4361; -.
DR EchoBASE; EB3067; -.
DR eggNOG; COG1566; Bacteria.
DR HOGENOM; CLU_018816_15_0_6; -.
DR InParanoid; P52599; -.
DR OMA; KEVQITH; -.
DR PhylomeDB; P52599; -.
DR BioCyc; EcoCyc:G7233-MON; -.
DR BioCyc; MetaCyc:G7233-MON; -.
DR PRO; PR:P52599; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990281; C:efflux pump complex; IC:ComplexPortal.
DR GO; GO:0098567; C:periplasmic side of plasma membrane; IC:ComplexPortal.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015721; P:bile acid and bile salt transport; IMP:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:EcoCyc.
DR GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
DR GO; GO:0140330; P:xenobiotic detoxification by transmembrane export across the cell outer membrane; IC:ComplexPortal.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IDA:EcoCyc.
DR InterPro; IPR043602; CusB_dom_1.
DR InterPro; IPR005694; Efflux_pump_mem.
DR InterPro; IPR032317; HlyD_D23.
DR Pfam; PF00529; CusB_dom_1; 1.
DR Pfam; PF16576; HlyD_D23; 1.
DR TIGRFAMs; TIGR00998; 8a0101; 1.
PE 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..387
FT /note="Probable multidrug resistance protein EmrK"
FT /id="PRO_0000201871"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..387
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 387 AA; 42585 MW; ABAD26F5D68FF38F CRC64;
MEQINSNKKH SNRRKYFSLL AVVLFIAFSG AYAYWSMELE DMISTDDAYV TGNADPISAQ
VSGSVTVVNH KDTNYVRQGD ILVSLDKTDA TIALNKAKNN LANIVRQTNK LYLQDKQYSA
EVASARIQYQ QSLEDYNRRV PLAKQGVISK ETLEHTKDTL ISSKAALNAA IQAYKANKAL
VMNTPLNRQP QVVEAADATK EAWLALKRTD IKSPVTGYIA QRSVQVGETV SPGQSLMAVV
PARQMWVNAN FKETQLTDVR IGQSVNIISD LYGENVVFHG RVTGINMGTG NAFSLLPAQN
ATGNWIKIVQ RVPVEVSLDP KELMEHPLRI GLSMTATIDT KNEDIAEMPE LASTVTSMPA
YTSKALVIDT SPIEKEISNI ISHNGQL
