MDTO_ECOL6
ID MDTO_ECOL6 Reviewed; 683 AA.
AC Q8FAX2;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Multidrug resistance protein MdtO;
GN Name=mdtO; OrderedLocusNames=c5086;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Could be involved in resistance to puromycin, acriflavine and
CC tetraphenylarsonium chloride. {ECO:0000250}.
CC -!- SUBUNIT: Could be part of a tripartite efflux system composed of MdtN,
CC MdtO and MdtP. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MdtO family. {ECO:0000305}.
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DR EMBL; AE014075; AAN83511.1; -; Genomic_DNA.
DR RefSeq; WP_001275175.1; NC_004431.1.
DR AlphaFoldDB; Q8FAX2; -.
DR STRING; 199310.c5086; -.
DR EnsemblBacteria; AAN83511; AAN83511; c5086.
DR KEGG; ecc:c5086; -.
DR eggNOG; COG1289; Bacteria.
DR HOGENOM; CLU_023392_1_0_6; -.
DR OMA; QSDWRIT; -.
DR BioCyc; ECOL199310:C5086-MON; -.
DR Proteomes; UP000001410; 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:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR InterPro; IPR006726; PHBA_efflux_AaeB/fusaric-R.
DR Pfam; PF04632; FUSC; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Cell inner membrane; Cell membrane; Membrane;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..683
FT /note="Multidrug resistance protein MdtO"
FT /id="PRO_0000210090"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 683 AA; 76268 MW; 0413891A0E01DB05 CRC64;
MSALNSLPLP VVRLLAFFHE ELSERRPGRV PQTMQLWVGC LLVILISMTF EIPFVALSLA
VLFYGIQSNA FYTKFVAILF VVATVLEIAS LFLIYKWSYG EPLIRLIIAG PILMSCMFLM
RTHRLGLVFF AVAIVAIYGQ TFPAMLDYPE AVVRLTLWCI VVGLYPTLLM TLIGVLWFPS
RAITQMHQAL NDRLDDAISH LTDSLAPLPE TRIEREALAL QKLNVFCLAD DANWRTQSAW
WQSCVATVTY IYSTLNRYDP TSFADSQAII EFRQKLASEI NKLQHSITEG QCWQSDWRIS
ESEAMTAREC NLENICQTLL QLGQMDPNTP PTPAAKPPSM VADAFTNPDY MRYAVKTLLA
CLICYTFYSG VDWEGIHTCM LTCVIVANPN VGSSYQKMVL RFGGAFCGAI LALLFTLLVM
PWLDNIVELL FVLAPIFLLG AWIATSSERS SYIGTQMVVT FALATLENVF GPVYDLVEIR
DRALGIIIGT VVSAVIYTFV WPESEARTLP QKLAGALGML SKVMRIPRQQ EVTALRTYLH
IRIGLHAAFN ACEEMCQRVV LERQLDSEER ALLIERSQTV IRQGRDILHA WDATWNSAQA
LDNALQPDRA GQFADALEKY AAGVATALSH SPQITLEETS ASQAILPTLL KQEQHVCQLF
ARLPDWTAPA LTPATEQAQG ATQ