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P76399 (MDTC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Multidrug resistance protein MdtC
Alternative name(s):
Multidrug transporter MdtC
Gene names
Name:mdtC
Synonyms:yegO
Ordered Locus Names:b2076, JW2061
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length1025 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The MdtABC tripartite complex confers resistance against novobiocin and deoxycholate. Ref.1 Ref.5

Subunit structure

Part of a tripartite efflux system composed of MdtA, MdtB and MdtC. MdtC forms a heteromultimer with MdtB.

Subcellular location

Cell inner membrane; Multi-pass membrane protein HAMAP-Rule MF_01424.

Induction

The mdtABC operon is transcriptionally activated by BaeR. Ref.1 Ref.5

Miscellaneous

MdtABC requires TolC for its function. HAMAP-Rule MF_01424

Sequence similarities

Belongs to the AcrB/AcrD/AcrF (TC 2.A.6) family. [View classification]

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

mdtBP763983EBI-1116694,EBI-561416

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10251025Multidrug resistance protein MdtC HAMAP-Rule MF_01424
PRO_0000161831

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2923Helical; Potential
Topological domain30 – 335306Periplasmic Potential
Transmembrane336 – 35318Helical; Potential
Topological domain354 – 3596Cytoplasmic Potential
Transmembrane360 – 37920Helical; Potential
Topological domain380 – 3889Periplasmic Potential
Transmembrane389 – 41123Helical; Potential
Topological domain412 – 43019Cytoplasmic Potential
Transmembrane431 – 45323Helical; Potential
Topological domain454 – 46714Periplasmic Potential
Transmembrane468 – 49023Helical; Potential
Topological domain491 – 852362Cytoplasmic Potential
Transmembrane853 – 87523Helical; Potential
Topological domain876 – 89419Periplasmic Potential
Transmembrane895 – 91723Helical; Potential
Topological domain918 – 94730Cytoplasmic Potential
Transmembrane948 – 97023Helical; Potential
Topological domain971 – 98414Periplasmic Potential
Transmembrane985 – 100723Helical; Potential
Topological domain1008 – 102518Cytoplasmic Potential

Sequences

Sequence LengthMass (Da)Tools
P76399 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: EF00BB4E7B301008

FASTA1,025111,010
        10         20         30         40         50         60 
MKFFALFIYR PVATILLSVA ITLCGILGFR MLPVAPLPQV DFPVIIVSAS LPGASPETMA 

        70         80         90        100        110        120 
SSVATPLERS LGRIAGVSEM TSSSSLGSTR IILQFDFDRD INGAARDVQA AINAAQSLLP 

       130        140        150        160        170        180 
SGMPSRPTYR KANPSDAPIM ILTLTSDTYS QGELYDFAST QLAPTISQID GVGDVDVGGS 

       190        200        210        220        230        240 
SLPAVRVGLN PQALFNQGVS LDDVRTAVSN ANVRKPQGAL EDGTHRWQIQ TNDELKTAAE 

       250        260        270        280        290        300 
YQPLIIHYNN GGAVRLGDVA TVTDSVQDVR NAGMTNAKPA ILLMIRKLPE ANIIQTVDSI 

       310        320        330        340        350        360 
RAKLPELQET IPAAIDLQIA QDRSPTIRAS LEEVEQTLII SVALVILVVF LFLRSGRATI 

       370        380        390        400        410        420 
IPAVSVPVSL IGTFAAMYLC GFSLNNLSLM ALTIATGFVV DDAIVVLENI ARHLEAGMKP 

       430        440        450        460        470        480 
LQAALQGTRE VGFTVLSMSL SLVAVFLPLL LMGGLPGRLL REFAVTLSVA IGISLLVSLT 

       490        500        510        520        530        540 
LTPMMCGWML KASKPREQKR LRGFGRMLVA LQQGYGKSLK WVLNHTRLVG VVLLGTIALN 

       550        560        570        580        590        600 
IWLYISIPKT FFPEQDTGVL MGGIQADQSI SFQAMRGKLQ DFMKIIRDDP AVDNVTGFTG 

       610        620        630        640        650        660 
GSRVNSGMMF ITLKPRDERS ETAQQIIDRL RVKLAKEPGA NLFLMAVQDI RVGGRQSNAS 

       670        680        690        700        710        720 
YQYTLLSDDL AALREWEPKI RKKLATLPEL ADVNSDQQDN GAEMNLVYDR DTMARLGIDV 

       730        740        750        760        770        780 
QAANSLLNNA FGQRQISTIY QPMNQYKVVM EVDPRYTQDI SALEKMFVIN NEGKAIPLSY 

       790        800        810        820        830        840 
FAKWQPANAP LSVNHQGLSA ASTISFNLPT GKSLSDASAA IDRAMTQLGV PSTVRGSFAG 

       850        860        870        880        890        900 
TAQVFQETMN SQVILIIAAI ATVYIVLGIL YESYVHPLTI LSTLPSAGVG ALLALELFNA 

       910        920        930        940        950        960 
PFSLIALIGI MLLIGIVKKN AIMMVDFALE AQRHGNLTPQ EAIFQACLLR FRPIMMTTLA 

       970        980        990       1000       1010       1020 
ALFGALPLVL SGGDGSELRQ PLGITIVGGL VMSQLLTLYT TPVVYLFFDR LRLRFSRKPK 


QTVTE 

« Hide

References

« Hide 'large scale' references
[1]"The putative response regulator BaeR stimulates multidrug resistance of Escherichia coli via a novel multidrug exporter system, MdtABC."
Nagakubo S., Nishino K., Hirata T., Yamaguchi A.
J. Bacteriol. 184:4161-4167(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION.
Strain: K12.
[2]"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. expand/collapse author list , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"The baeSR two-component regulatory system activates transcription of the yegMNOB (mdtABCD) transporter gene cluster in Escherichia coli and increases its resistance to novobiocin and deoxycholate."
Baranova N., Nikaido H.
J. Bacteriol. 184:4168-4176(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[6]"Global topology analysis of the Escherichia coli inner membrane proteome."
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: K12 / MG1655 / ATCC 47076.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB089189 Genomic DNA. Translation: BAC06609.1.
U00096 Genomic DNA. Translation: AAC75137.1.
AP009048 Genomic DNA. Translation: BAA15932.1.
PIRC64974.
RefSeqNP_416580.1. NC_000913.2.
YP_490318.1. NC_007779.1.

3D structure databases

ProteinModelPortalP76399.
SMRP76399. Positions 6-998.
ModBaseSearch...

Protein-protein interaction databases

IntActP76399. 4 interactions.
STRING511145.b2076.

Protein family/group databases

TCDB2.A.6.2.14. resistance-nodulation-cell division (RND) superfamily.

Proteomic databases

PRIDEP76399.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75137; AAC75137; b2076.
BAA15932; BAA15932; BAA15932.
GeneID12931428.
946608.
KEGGecj:Y75_p2039.
eco:b2076.
PATRIC32119485. VBIEscCol129921_2153.

Organism-specific databases

EchoBASEEB3811.
EcoGeneEG14058. mdtC.

Phylogenomic databases

eggNOGCOG0841.
HOGENOMHOG000158127.
KOK07789.
OMAGQLYDFA.
ProtClustDBPRK10614.

Enzyme and pathway databases

BioCycEcoCyc:B2076-MONOMER.
ECOL316407:JW2061-MONOMER.

Gene expression databases

GenevestigatorP76399.

Family and domain databases

Gene3D3.30.2090.10. 2 hits.
HAMAPMF_01424. MdtC.
InterProIPR027463. AcrB_DN_DC_subdom.
IPR001036. Acrflvin-R.
IPR023931. Multidrug-R_MdtC.
[Graphical view]
PfamPF00873. ACR_tran. 1 hit.
[Graphical view]
PRINTSPR00702. ACRIFLAVINRP.
SUPFAMSSF82714. SSF82714. 2 hits.
ProtoNetSearch...

Entry information

Entry nameMDTC_ECOLI
AccessionPrimary (citable) accession number: P76399
Secondary accession number(s): O08006
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: May 29, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families