MDTL_ECOBW
ID MDTL_ECOBW Reviewed; 391 AA.
AC C4ZYY8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Multidrug resistance protein MdtL {ECO:0000255|HAMAP-Rule:MF_01530};
GN Name=mdtL {ECO:0000255|HAMAP-Rule:MF_01530}; OrderedLocusNames=BWG_3401;
OS Escherichia coli (strain K12 / MC4100 / BW2952).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=595496;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MC4100 / BW2952;
RX PubMed=19376874; DOI=10.1128/jb.00118-09;
RA Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA Wang L.;
RT "Genomic sequencing reveals regulatory mutations and recombinational events
RT in the widely used MC4100 lineage of Escherichia coli K-12.";
RL J. Bacteriol. 191:4025-4029(2009).
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}.
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DR EMBL; CP001396; ACR63815.1; -; Genomic_DNA.
DR RefSeq; WP_000085982.1; NC_012759.1.
DR AlphaFoldDB; C4ZYY8; -.
DR SMR; C4ZYY8; -.
DR KEGG; ebw:BWG_3401; -.
DR HOGENOM; CLU_001265_47_1_6; -.
DR OMA; AGSCYVV; -.
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_1000215399"
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 203..222
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01530"
SQ SEQUENCE 391 AA; 41490 MW; F1CD02E113AA94B7 CRC64;
MSRFLICSFA LVLLYPAGID MYLVGLPRIA ADLNASEAQL HIAFSVYLAG MAAAMLFAGK
VADRSGRKPV AIPGAALFII ASVFCSLAET STLFLAGRFL QGLGAGCCYV VAFAILRDTL
DDRRRAKVLS LLNGITCIIP VLAPVLGHLI MLKFPWQSLF WAMAMMGIAV LMLSLFILKE
TRPAAPAASD KPRENSESLL NRFFLSRVVI TTLSVSVILT FVNTSPVLLM EIMGFERGEY
ATIMALTAGV SMTVSFSTPF ALGIFKPRTL MITSQVLFLA AGITLAVSPS HAVSLFGITL
ICAGFSVGFG VAMSQALGPF SLRAGVASST LGIAQVCGSS LWIWLAAVVG IGAWNMLIGI
LIACSIVSLL LIMFVAPGRP VAAHEEIHHH A