MDTL_ECOUT
ID MDTL_ECOUT Reviewed; 391 AA.
AC Q1R4M4;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Multidrug resistance protein MdtL {ECO:0000255|HAMAP-Rule:MF_01530};
GN Name=mdtL {ECO:0000255|HAMAP-Rule:MF_01530}; OrderedLocusNames=UTI89_C4263;
OS Escherichia coli (strain UTI89 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=364106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTI89 / UPEC;
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA Gordon J.I.;
RT "Identification of genes subject to positive selection in uropathogenic
RT strains of Escherichia coli: a comparative genomics approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC -!- FUNCTION: Confers resistance to chloramphenicol. {ECO:0000255|HAMAP-
CC Rule:MF_01530}.
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}.
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; CP000243; ABE09690.1; -; Genomic_DNA.
DR RefSeq; WP_000085964.1; NC_007946.1.
DR AlphaFoldDB; Q1R4M4; -.
DR SMR; Q1R4M4; -.
DR EnsemblBacteria; ABE09690; ABE09690; UTI89_C4263.
DR KEGG; eci:UTI89_C4263; -.
DR HOGENOM; CLU_001265_47_1_6; -.
DR OMA; AGSCYVV; -.
DR Proteomes; UP000001952; 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 GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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 Antibiotic resistance; Cell inner membrane; Cell membrane; Membrane;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..391
FT /note="Multidrug resistance protein MdtL"
FT /id="PRO_0000281998"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TOPO_DOM 25..41
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TOPO_DOM 63..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TOPO_DOM 90..92
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TOPO_DOM 114..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TOPO_DOM 152..157
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TOPO_DOM 179..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..222
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TOPO_DOM 223..244
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TOPO_DOM 266..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TOPO_DOM 290..292
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TOPO_DOM 314..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TOPO_DOM 352..355
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TOPO_DOM 377..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 391 AA; 41534 MW; EAB7743994677BBD CRC64;
MSRFLICSFA LVLLYPAGID MYLVGLPRIA ADLNASEAQL HIAFSVYLAG MAAAMLFAGK
VADRSGRKPV AIPGAALFII ASVFCSLAET SALFLAGRFL QGLGAGCCYV VAFAILRDTL
DDRRRAKVLS LLNGITCIIP VLAPVLGHLI MLKFPWQSLF WTMATMGIAL LMLSLFILKE
TRPAAPTTSD KPRENSESLL NRFFLSRVVI TTLSVSVILT FVNTSPVLLM EIMGFERGEY
ATIMALTAGV SMTVSFSTPF ALGIFKPRTL MITSQVLFLA AGITLAVSPS HAVSLFGITL
ICAGFSVGFG VAMSQALGPF SLRAGVASST LGIAQVCGSS LWIWLAAVVG IGAWNMLIGI
LIACSIVSLL LIMFVAPGRP VAAHEEIHHH A