MDTL_SALA4
ID MDTL_SALA4 Reviewed; 395 AA.
AC B5EYX7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Multidrug resistance protein MdtL {ECO:0000255|HAMAP-Rule:MF_01530};
GN Name=mdtL {ECO:0000255|HAMAP-Rule:MF_01530}; OrderedLocusNames=SeAg_B4071;
OS Salmonella agona (strain SL483).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL483;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01530}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01530}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family.
CC MdtL (TC 2.A.1.2.22) subfamily. {ECO:0000255|HAMAP-Rule:MF_01530}.
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DR EMBL; CP001138; ACH52347.1; -; Genomic_DNA.
DR RefSeq; WP_000819614.1; NC_011149.1.
DR AlphaFoldDB; B5EYX7; -.
DR SMR; B5EYX7; -.
DR EnsemblBacteria; ACH52347; ACH52347; SeAg_B4071.
DR KEGG; sea:SeAg_B4071; -.
DR HOGENOM; CLU_001265_47_1_6; -.
DR OMA; AGSCYVV; -.
DR Proteomes; UP000008819; 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:UniProtKB-UniRule.
DR HAMAP; MF_01530; MFS_MdtL; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR023697; Multidrug-R_MdtL.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..395
FT /note="Multidrug resistance protein MdtL"
FT /id="PRO_1000200826"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
SQ SEQUENCE 395 AA; 41945 MW; 9D6E5DAA97A9C347 CRC64;
MKRFLLCSFA LVLLYPAGID MYLVGLPRIA ADLNASEAQL HIAFSVYLAG MATAMLFAGK
IADQSGRKPV AIVGALVFMM ASLLCSRASE GSLFLSGRFL QGVGAGGCYV VAFAILRDTL
DEHRRAKVLS LLNGITCIVP VLAPVVGHLI MLRFPWQSLF YTMSAMGIIV GLLSLFILRE
TRPARLAPRD LSRSSPAAES LVNRFFVSRL AITTLSVSVI LTFVNASPVL LMEVMGFSRG
DYAITMALTA GVSMVVSFST PFALGLFKPR TLMLVSQGLF LTAGVTLSLA HTNTVTLFGL
TLICAGFSVG FGVAMSQALG PFSLRAGVAS STLGIAQVCG SSLWIWLAAI LGISAMNMLI
GILIGCSIVS ILLIFSVAPN RSVAEHEEIP YQSRS