MDTG_ECO24
ID MDTG_ECO24 Reviewed; 408 AA.
AC A7ZKF6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Multidrug resistance protein MdtG {ECO:0000255|HAMAP-Rule:MF_01528};
GN Name=mdtG {ECO:0000255|HAMAP-Rule:MF_01528};
GN OrderedLocusNames=EcE24377A_1174;
OS Escherichia coli O139:H28 (strain E24377A / ETEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331111;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E24377A / ETEC;
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: Confers resistance to fosfomycin and deoxycholate.
CC {ECO:0000255|HAMAP-Rule:MF_01528}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01528}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01528}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family.
CC MdtG (TC 2.A.1.2.20) subfamily. {ECO:0000255|HAMAP-Rule:MF_01528}.
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DR EMBL; CP000800; ABV18113.1; -; Genomic_DNA.
DR RefSeq; WP_000074172.1; NC_009801.1.
DR AlphaFoldDB; A7ZKF6; -.
DR SMR; A7ZKF6; -.
DR EnsemblBacteria; ABV18113; ABV18113; EcE24377A_1174.
DR GeneID; 66670680; -.
DR KEGG; ecw:EcE24377A_1174; -.
DR HOGENOM; CLU_001265_57_3_6; -.
DR OMA; VIRHNVP; -.
DR Proteomes; UP000001122; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 2.
DR HAMAP; MF_01528; MFS_MdtG; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR023692; Mutidrug-R_MdtG.
DR InterPro; IPR001958; Tet-R_TetA/multi-R_MdtG.
DR Pfam; PF07690; MFS_1; 1.
DR PRINTS; PR01035; TCRTETA.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Cell inner membrane; Cell membrane; Membrane;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..408
FT /note="Multidrug resistance protein MdtG"
FT /id="PRO_1000068674"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01528"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01528"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01528"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01528"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01528"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01528"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01528"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01528"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01528"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01528"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01528"
SQ SEQUENCE 408 AA; 43867 MW; C07B719D54A28D27 CRC64;
MSPCENDTPI NWKRNLIVAW LGCFLTGAAF SLVMPFLPLY VEQLGVTGHS ALNMWSGIVF
SITFLFSAIA SPFWGGLADR KGRKLMLLRS ALGMGIVMVL MGLAQNIWQF LILRALLGLL
GGFVPNANAL IATQVPRNKS GWALGTLSTG GVSGALLGPM AGGLLADSYG LRPVFFITAS
VLILCFFVTL FCIREKFQPV SKKEMLHMRE VVTSLKNPKL VLSLFVTTLI IQVATGSIAP
ILTLYVRELA GNVSNVAFIS GMIASVPGVA ALLSAPRLGK LGDRIGPEKI LITALIFSVL
LLIPMSYVQT PLQLGILRFL LGAADGALLP AVQTLLVYNS SNQIAGRIFS YNQSFRDIGN
VTGPLMGAAI SANYGFRAVF LVTAGVVLFN AVYSWNSLRR RRIPQVSN