ID A0A248KHX3_9ENTR Unreviewed; 393 AA.
AC A0A248KHX3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Multidrug resistance protein MdtA {ECO:0000256|HAMAP-Rule:MF_01422};
DE AltName: Full=Multidrug transporter MdtA {ECO:0000256|HAMAP-Rule:MF_01422};
GN Name=mdtA {ECO:0000256|HAMAP-Rule:MF_01422};
GN ORFNames=CEW81_08665 {ECO:0000313|EMBL:ASG63129.1};
OS Kluyvera genomosp. 3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Kluyvera.
OX NCBI_TaxID=2774055 {ECO:0000313|EMBL:ASG63129.1, ECO:0000313|Proteomes:UP000197098};
RN [1] {ECO:0000313|EMBL:ASG63129.1, ECO:0000313|Proteomes:UP000197098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YDC799 {ECO:0000313|EMBL:ASG63129.1,
RC ECO:0000313|Proteomes:UP000197098};
RA Ito R., Pacey M.P., Doi Y.;
RT "Origin of plasmid-mediated fosfomycin resistance gene fosA3.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Part of a tripartite efflux system composed of MdtA, MdtB and
CC MdtC. {ECO:0000256|HAMAP-Rule:MF_01422}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01422}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01422}.
CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC family. {ECO:0000256|ARBA:ARBA00009477, ECO:0000256|HAMAP-
CC 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; CP022114; ASG63129.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A248KHX3; -.
DR KEGG; kgo:CEW81_08665; -.
DR Proteomes; UP000197098; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.30.170; -; 1.
DR Gene3D; 2.40.420.20; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 1.10.287.470; Helix hairpin bin; 1.
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 NCBIfam; TIGR01730; RND_mfp; 1.
DR PANTHER; PTHR30469; MULTIDRUG RESISTANCE PROTEIN MDTA; 1.
DR PANTHER; PTHR30469:SF12; MULTIDRUG RESISTANCE PROTEIN MDTA; 1.
DR Pfam; PF13533; Biotin_lipoyl_2; 1.
DR Pfam; PF13437; HlyD_3; 1.
DR SUPFAM; SSF111369; HlyD-like secretion proteins; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01422};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01422}; Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01422};
KW Reference proteome {ECO:0000313|Proteomes:UP000197098};
KW Transport {ECO:0000256|HAMAP-Rule:MF_01422}.
FT DOMAIN 65..113
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 105..132
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 393 AA; 41250 MW; B6A0887AA7BA95C2 CRC64;
MWHFSSNSDT SGSTAAKPAG APSAGGGRHG GRFGGALAPV QAATATSEAV PRYLSGLGTI
TAANTVTVRS RVDGQLMAIH FQEGQQVKAG DLLAEIDPSQ FKVALAQAQG QLAKDKATLA
NARRDLARYQ QLVKTNLVSR QELDTQQSLV SETEGTIKAD QAAVASAQLQ LDWSRITAPI
DGRVGLKQVD IGNQISSGDT TGIVVLTQTH PIDLVFTLPE NDIATVVAAQ KAGKTLVVEA
WDRTNKQKLS EGTLLSLDNQ IDATTGTIKL KARFNNQDDA LFPNQFVNAR MLVDTQQNAV
VIPTAALQMG NDGHFVWVLN SDNKVSKHTV IPGIQDSQKV VIDAGLSAGD RVVTDGIDRL
TEGAKVEVVT AHDASTAGAE KPAAAAGHKG ARG
//