MDTA_ECOHS
ID MDTA_ECOHS Reviewed; 415 AA.
AC A8A1U6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Multidrug resistance protein MdtA {ECO:0000255|HAMAP-Rule:MF_01422};
DE AltName: Full=Multidrug transporter MdtA {ECO:0000255|HAMAP-Rule:MF_01422};
DE Flags: Precursor;
GN Name=mdtA {ECO:0000255|HAMAP-Rule:MF_01422}; OrderedLocusNames=EcHS_A2216;
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_01422}.
CC -!- SUBUNIT: Part of a tripartite efflux system composed of MdtA, MdtB and
CC MdtC. {ECO:0000255|HAMAP-Rule:MF_01422}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01422}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01422}.
CC -!- INDUCTION: The mdtABC operon is transcriptionally activated by BaeR.
CC {ECO:0000255|HAMAP-Rule:MF_01422}.
CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC family. {ECO:0000255|HAMAP-Rule:MF_01422}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000802; ABV06500.1; -; Genomic_DNA.
DR RefSeq; WP_000678989.1; NC_009800.1.
DR AlphaFoldDB; A8A1U6; -.
DR SMR; A8A1U6; -.
DR KEGG; ecx:EcHS_A2216; -.
DR HOGENOM; CLU_018816_2_0_6; -.
DR OMA; GQLMAIH; -.
DR Proteomes; UP000001123; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01422; MdtA; 1.
DR InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR InterPro; IPR022824; Multidrug-R_MdtA.
DR InterPro; IPR006143; RND_pump_MFP.
DR Pfam; PF13533; Biotin_lipoyl_2; 1.
DR TIGRFAMs; TIGR01730; RND_mfp; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Signal; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01422"
FT CHAIN 22..415
FT /note="Multidrug resistance protein MdtA"
FT /id="PRO_1000068499"
FT REGION 32..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 44464 MW; 26240DBBE0DE1A5F CRC64;
MKGSYKSRWV IVIVVVIAAI AAFWFWQGRN DSRSAAPGAT KQAQQSPAGG RRGMRSGPLA
PVQAATAVEQ AVPRYLTGLG TITAANTVTV RSRVDGQLIA LHFQEGQQVK AGDLLAEIDP
SQFKVALAQA QGQLAKDKAT LANARRDLAR YQQLAKTNLV SRQELDAQQA LVSETEGTIK
ADEASVASAQ LQLDWSRITA PVDGRVGLKQ VDVGNQISSG DTTGIVVITQ THPIDLVFTL
PESDIATVVQ AQKAGKPLVV EAWDRTNSKK LSEGTLLSLD NQIDATTGTI KVKARFNNQD
DALFPNQFVN ARMLVDTEQN AVVIPTAALQ MGNEGHFVWV LNSENKVSKH LVTPGIQDSQ
KVVIRAGISA GDRVVTDGID RLTEGAKVEV VEAQSATTPE EKATSREYAK KGARS