MDTC_ECOSE
ID MDTC_ECOSE Reviewed; 1025 AA.
AC B6HYS1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 25-MAY-2022, entry version 72.
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}; OrderedLocusNames=ECSE_2349;
OS Escherichia coli (strain SE11).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=409438;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SE11;
RX PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T.,
RA Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT "Complete genome sequence and comparative analysis of the wild-type
RT commensal Escherichia coli strain SE11 isolated from a healthy adult.";
RL DNA Res. 15:375-386(2008).
CC -!- FUNCTION: The MdtABC tripartite complex confers resistance against
CC novobiocin and deoxycholate. {ECO:0000255|HAMAP-Rule:MF_01424}.
CC -!- SUBUNIT: Part of a tripartite efflux system composed of MdtA, MdtB and
CC MdtC. MdtC forms a heteromultimer with MdtB. {ECO:0000255|HAMAP-
CC Rule:MF_01424}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01424}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01424}.
CC -!- INDUCTION: The mdtABC operon is transcriptionally activated by BaeR.
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; AP009240; BAG77873.1; -; Genomic_DNA.
DR RefSeq; WP_000667549.1; NC_011415.1.
DR AlphaFoldDB; B6HYS1; -.
DR SMR; B6HYS1; -.
DR EnsemblBacteria; BAG77873; BAG77873; ECSE_2349.
DR GeneID; 66674024; -.
DR KEGG; ecy:ECSE_2349; -.
DR HOGENOM; CLU_002755_1_2_6; -.
DR OMA; WRGVRTD; -.
DR Proteomes; UP000008199; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProtKB-UniRule.
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 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1025
FT /note="Multidrug resistance protein MdtC"
FT /id="PRO_1000145672"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT TRANSMEM 853..873
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT TRANSMEM 875..895
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT TRANSMEM 897..917
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT TRANSMEM 953..973
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
FT TRANSMEM 984..1004
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01424"
SQ SEQUENCE 1025 AA; 111055 MW; 370BB6F001FF649A CRC64;
MKFFALFIYR PVATILLSVA ITLCGILGFR MLPVAPLPQV DFPVIMVSAS LPGASPETMA
SSVATPLERS LGRIAGVSEM TSSSSLGSTR IILQFDFDRD INGAARDVQA AINAAQSLLP
SGMPSRPTYR KANPSDAPIM ILTLTSDTYS QGELYDFAST QLAPTISQID GVGDVDVGGS
SLPAVRVGLN PQALFNQGVS LDDVRTAISN ANVRKPQGAL EDGTHRWQIQ TNDELKTAAE
YQPLIIHYNN GGAVRLGDVA TVTDSVQDVR NAGMTNAKPA ILLMIRKLPE ANIIQTVDSI
RAKLPELQET IPAAIDLQIA QDRSPTIRAS LEEVEQTLII SVALVILVVF LFLRSGRATI
IPAVVVPVSL 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