MDTC_ECOLI
ID MDTC_ECOLI Reviewed; 1025 AA.
AC P76399; O08006;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Multidrug resistance protein MdtC {ECO:0000255|HAMAP-Rule:MF_01424};
DE AltName: Full=Multidrug transporter MdtC {ECO:0000255|HAMAP-Rule:MF_01424};
GN Name=mdtC {ECO:0000255|HAMAP-Rule:MF_01424}; Synonyms=yegO;
GN OrderedLocusNames=b2076, JW2061;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=12107133; DOI=10.1128/jb.184.15.4161-4167.2002;
RA Nagakubo S., Nishino K., Hirata T., Yamaguchi A.;
RT "The putative response regulator BaeR stimulates multidrug resistance of
RT Escherichia coli via a novel multidrug exporter system, MdtABC.";
RL J. Bacteriol. 184:4161-4167(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
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 FUNCTION, AND INDUCTION.
RX PubMed=12107134; DOI=10.1128/jb.184.15.4168-4176.2002;
RA Baranova N., Nikaido H.;
RT "The baeSR two-component regulatory system activates transcription of the
RT yegMNOB (mdtABCD) transporter gene cluster in Escherichia coli and
RT increases its resistance to novobiocin and deoxycholate.";
RL J. Bacteriol. 184:4168-4176(2002).
RN [6]
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: The MdtABC tripartite complex confers resistance against
CC novobiocin and deoxycholate. MdtABC requires TolC for its function.
CC {ECO:0000255|HAMAP-Rule:MF_01424, ECO:0000269|PubMed:12107133,
CC ECO:0000269|PubMed:12107134}.
CC -!- SUBUNIT: Part of a tripartite efflux system composed of MdtA, MdtB and
CC MdtC. MdtC forms a heteromultimer with MdtB.
CC -!- INTERACTION:
CC P76399; P76398: mdtB; NbExp=4; IntAct=EBI-1116694, EBI-561416;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- INDUCTION: The mdtABC operon is transcriptionally activated by BaeR.
CC {ECO:0000255|HAMAP-Rule:MF_01424, ECO:0000269|PubMed:12107133,
CC ECO:0000269|PubMed:12107134}.
CC -!- SIMILARITY: Belongs to the resistance-nodulation-cell division (RND)
CC (TC 2.A.6) family. MdtC subfamily. {ECO:0000255|HAMAP-Rule:MF_01424}.
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DR EMBL; AB089189; BAC06609.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75137.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15932.1; -; Genomic_DNA.
DR PIR; C64974; C64974.
DR RefSeq; NP_416580.1; NC_000913.3.
DR RefSeq; WP_000667481.1; NZ_LN832404.1.
DR AlphaFoldDB; P76399; -.
DR SMR; P76399; -.
DR BioGRID; 4260422; 177.
DR ComplexPortal; CPX-2119; MdtABC-TolC multidrug efflux transport complex.
DR IntAct; P76399; 4.
DR STRING; 511145.b2076; -.
DR TCDB; 2.A.6.2.12; the resistance-nodulation-cell division (rnd) superfamily.
DR PaxDb; P76399; -.
DR PRIDE; P76399; -.
DR EnsemblBacteria; AAC75137; AAC75137; b2076.
DR EnsemblBacteria; BAA15932; BAA15932; BAA15932.
DR GeneID; 946608; -.
DR KEGG; ecj:JW2061; -.
DR KEGG; eco:b2076; -.
DR PATRIC; fig|1411691.4.peg.174; -.
DR EchoBASE; EB3811; -.
DR eggNOG; COG0841; Bacteria.
DR HOGENOM; CLU_002755_1_2_6; -.
DR InParanoid; P76399; -.
DR OMA; WRGVRTD; -.
DR PhylomeDB; P76399; -.
DR BioCyc; EcoCyc:B2076-MON; -.
DR BioCyc; MetaCyc:B2076-MON; -.
DR PRO; PR:P76399; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990281; C:efflux pump complex; IC:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0098567; C:periplasmic side of plasma membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015125; F:bile acid transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015721; P:bile acid and bile salt transport; IMP:EcoCyc.
DR GO; GO:0140330; P:xenobiotic detoxification by transmembrane export across the cell outer membrane; IC:ComplexPortal.
DR GO; GO:0042908; P:xenobiotic transport; IMP:EcoCyc.
DR Gene3D; 3.30.2090.10; -; 2.
DR HAMAP; MF_01424; MdtC; 1.
DR InterPro; IPR027463; AcrB_DN_DC_subdom.
DR InterPro; IPR001036; Acrflvin-R.
DR InterPro; IPR023931; Multidrug-R_MdtC.
DR PANTHER; PTHR32063; PTHR32063; 1.
DR Pfam; PF00873; ACR_tran; 1.
DR PRINTS; PR00702; ACRIFLAVINRP.
DR SUPFAM; SSF82714; SSF82714; 2.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1025
FT /note="Multidrug resistance protein MdtC"
FT /id="PRO_0000161831"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT TOPO_DOM 30..335
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..353
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT TOPO_DOM 354..359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..379
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT TOPO_DOM 380..388
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..411
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT TOPO_DOM 412..430
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..453
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT TOPO_DOM 454..467
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..490
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT TOPO_DOM 491..852
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 853..875
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT TOPO_DOM 876..894
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 895..917
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT TOPO_DOM 918..947
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 948..970
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT TOPO_DOM 971..984
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 985..1007
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT TOPO_DOM 1008..1025
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1025 AA; 111010 MW; EF00BB4E7B301008 CRC64;
MKFFALFIYR PVATILLSVA ITLCGILGFR MLPVAPLPQV DFPVIIVSAS LPGASPETMA
SSVATPLERS LGRIAGVSEM TSSSSLGSTR IILQFDFDRD INGAARDVQA AINAAQSLLP
SGMPSRPTYR KANPSDAPIM ILTLTSDTYS QGELYDFAST QLAPTISQID GVGDVDVGGS
SLPAVRVGLN PQALFNQGVS LDDVRTAVSN ANVRKPQGAL EDGTHRWQIQ TNDELKTAAE
YQPLIIHYNN GGAVRLGDVA TVTDSVQDVR NAGMTNAKPA ILLMIRKLPE ANIIQTVDSI
RAKLPELQET IPAAIDLQIA QDRSPTIRAS LEEVEQTLII SVALVILVVF LFLRSGRATI
IPAVSVPVSL IGTFAAMYLC GFSLNNLSLM ALTIATGFVV DDAIVVLENI ARHLEAGMKP
LQAALQGTRE VGFTVLSMSL SLVAVFLPLL LMGGLPGRLL REFAVTLSVA IGISLLVSLT
LTPMMCGWML KASKPREQKR LRGFGRMLVA LQQGYGKSLK WVLNHTRLVG VVLLGTIALN
IWLYISIPKT FFPEQDTGVL MGGIQADQSI SFQAMRGKLQ DFMKIIRDDP AVDNVTGFTG
GSRVNSGMMF ITLKPRDERS ETAQQIIDRL RVKLAKEPGA NLFLMAVQDI RVGGRQSNAS
YQYTLLSDDL AALREWEPKI RKKLATLPEL ADVNSDQQDN GAEMNLVYDR DTMARLGIDV
QAANSLLNNA FGQRQISTIY QPMNQYKVVM EVDPRYTQDI SALEKMFVIN NEGKAIPLSY
FAKWQPANAP LSVNHQGLSA ASTISFNLPT GKSLSDASAA IDRAMTQLGV PSTVRGSFAG
TAQVFQETMN SQVILIIAAI ATVYIVLGIL YESYVHPLTI LSTLPSAGVG ALLALELFNA
PFSLIALIGI MLLIGIVKKN AIMMVDFALE AQRHGNLTPQ EAIFQACLLR FRPIMMTTLA
ALFGALPLVL SGGDGSELRQ PLGITIVGGL VMSQLLTLYT TPVVYLFFDR LRLRFSRKPK
QTVTE
