MDTC_ECOHS
ID MDTC_ECOHS Reviewed; 1025 AA.
AC A8A1U8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=EcHS_A2218;
OS Escherichia coli O9:H4 (strain HS).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331112;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS;
RX PubMed=18676672; DOI=10.1128/jb.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(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; CP000802; ABV06502.1; -; Genomic_DNA.
DR RefSeq; WP_000667589.1; NC_009800.1.
DR AlphaFoldDB; A8A1U8; -.
DR SMR; A8A1U8; -.
DR KEGG; ecx:EcHS_A2218; -.
DR HOGENOM; CLU_002755_1_2_6; -.
DR OMA; WRGVRTD; -.
DR Proteomes; UP000001123; 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_1000068507"
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 469..489
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; 111067 MW; 01C3986895A752D9 CRC64;
MKFFALFIYR PVATILLSVA ITLCGILGFR MLPVAPLPQV DFPVIMVSAS 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 REFTVTLSVA 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 SGGDGSELRH PLGITIVGGL VMSQLLTLYT TPVVYLFFDR LRLRFSRKPK
QTVTE