MDTC_PANAA
ID MDTC_PANAA Reviewed; 1025 AA.
AC F2EYE0;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 43.
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=PAJ_1810;
OS Pantoea ananatis (strain AJ13355).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=932677;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AJ13355;
RX PubMed=22159605; DOI=10.1007/s00253-011-3713-5;
RA Hara Y., Kadotani N., Izui H., Katashkina J.I., Kuvaeva T.M.,
RA Andreeva I.G., Golubeva L.I., Malko D.B., Makeev V.J., Mashko S.V.,
RA Kozlov Y.I.;
RT "The complete genome sequence of Pantoea ananatis AJ13355, an organism with
RT great biotechnological potential.";
RL Appl. Microbiol. Biotechnol. 93:331-341(2012).
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 -!- SIMILARITY: Belongs to the resistance-nodulation-cell division (RND)
CC (TC 2.A.6) family. MdtC subfamily. {ECO:0000255|HAMAP-Rule:MF_01424}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAK11890.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP012032; BAK11890.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_028715330.1; NC_017531.2.
DR AlphaFoldDB; F2EYE0; -.
DR SMR; F2EYE0; -.
DR STRING; 932677.PAJ_1810; -.
DR EnsemblBacteria; BAK11890; BAK11890; PAJ_1810.
DR KEGG; paj:PAJ_1810; -.
DR PATRIC; fig|932677.3.peg.2114; -.
DR eggNOG; COG0841; Bacteria.
DR HOGENOM; CLU_002755_1_1_6; -.
DR BioCyc; PANA932677:PAJ_RS10025-MON; -.
DR Proteomes; UP000006690; 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 3: Inferred from homology;
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_0000414035"
FT TRANSMEM 16..36
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 459..479
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; 110488 MW; 49B339EA22C64D77 CRC64;
MKFFALFIHR PVATTLLTLA IALAGILGFR LLPVAPLPQV DFPVIMVSAS LPGASPETMA
SSVATPLERS LGRIAGVSEM TSTSSLGSTR IIMVFDFDRD INGAARDVQA AINAAQSLLP
TGMPSRPTYR KANPSDAPIM IMTLTSDLYS PAQLYDYAST QLAQKLSQIN GVGDVTVGGS
SLPAVRVALN PQALFNQGVS LDAVRQTISN ANQRRPQGAV EDGQQRWQLR TNDALQTASE
YQPLVVHYNN GAAVRLSDVA TVQDSVQDVR NAGMSRGKPA VLLVIRKTAD ANVIETVDRI
RAELPELHEI IPAAINLEVA QDRSPTIRAS LEEVEQSLMI AVALVILVVF VFLRSGRATL
IPAVAVPVSL IGTFAAMYLC GFSLNNLSLM ALTIATGFVV DDAIVVLENI ARHVEAGMKP
MAAALKGVRE VGFTVLSMSL SLIAVFLPLL MTGGLIGRFF AEFSITLSVA ILISLFVSVT
LTPMMCAYLL KPHAPRSQPQ RRGVGRLLLA VQRGYARSLT VVLNHARWVL LLLLGTVALT
VWLFISIPKT FLPEQDTGRL SGFISADQSI SFQAMRGKLE DFMKIVGADP DVSSVVGFTG
GMRTNMGLMF ISLKPLSERK DTAQAVIARL RAKLANEPGA NLYLNAVQDI RVGGREANAS
YQYSLLSDDL AALRTWEPKI RQAFTALPEL ADVNSDQQDK GSEMALTYDR ASMARLGINV
SEANALLNDA FGQRQISTIY QPLNQYKVVM EVDPRYTQDI SALNQMFVIN SEGKPIPLAW
FAKWQPANAP LSVNHEGLSA ASTISFNLPE GVSLSQASEA IERTMTALGV PSSVRGSFAG
TAQAFQQSQS SQLWLMLAAI AAVYIVLGIL YESYVHPLTI LSTLPSAGVG ALLALALFDT
PFSLIALIGI LLLIGIVKKN AIMMVDFALE AERNGNLSPR DAIFQACLLR FRPILMTTLA
ALFGALPLVL TSGDGAELRQ PLGITIAGGL IMSQLLTLYT TPVVYLMMDK LRRKKRTQTI
NATQH