MDTA_ECO8A
ID MDTA_ECO8A Reviewed; 415 AA.
AC B7M457;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=ECIAI1_2150;
OS Escherichia coli O8 (strain IAI1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585034;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI1;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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}.
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DR EMBL; CU928160; CAQ98996.1; -; Genomic_DNA.
DR RefSeq; WP_000678962.1; NC_011741.1.
DR AlphaFoldDB; B7M457; -.
DR SMR; B7M457; -.
DR PRIDE; B7M457; -.
DR KEGG; ecr:ECIAI1_2150; -.
DR HOGENOM; CLU_018816_2_0_6; -.
DR OMA; GQLMAIH; -.
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_1000145637"
FT REGION 31..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 31..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 44454 MW; FB811905A7BD9E2C CRC64;
MKGSYKSRWV IVIVVVIAAI AAFWFWQGRN DSQSAAPGAT KQAQQSPAGG RRGMRSGPLA
PVQAATAVEQ AVPRYLTGLG TITAANTVTV RSRVDGQLMA 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
