MDLB_ECOL6
ID MDLB_ECOL6 Reviewed; 593 AA.
AC P0AAG6; P30751; P75706; P77117;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Multidrug resistance-like ATP-binding protein MdlB;
DE EC=7.6.2.2;
GN Name=mdlB; OrderedLocusNames=c0566;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Drug exporter-2
CC (TC 3.A.1.117) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN79044.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AE014075; AAN79044.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001256201.1; NC_004431.1.
DR AlphaFoldDB; P0AAG6; -.
DR SMR; P0AAG6; -.
DR STRING; 199310.c0566; -.
DR EnsemblBacteria; AAN79044; AAN79044; c0566.
DR KEGG; ecc:c0566; -.
DR eggNOG; COG1132; Bacteria.
DR HOGENOM; CLU_000604_84_3_6; -.
DR OMA; MSVMMAT; -.
DR Proteomes; UP000001410; 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:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..593
FT /note="Multidrug resistance-like ATP-binding protein MdlB"
FT /id="PRO_0000092498"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 47..62
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 84..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 162..164
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 186..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 276..278
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 300..593
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..310
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 341..574
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 374..381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 593 AA; 65222 MW; CF1EE70009EB05D8 CRC64;
MRSFSQLWPT LKRLLAYGSP WRKPLGIAVL MMWVAAAAEV SGPLLISYFI DNMVAKNNLP
LKVVAGLAAA YVGLQLFAAG LHYAQSLLFN RAAVGVVQQL RTDVMDAALR QPLSEFDTQP
VGQVISRVTN DTEVIRDLYV TVVATVLRSA ALVGAMLVAM FSLDWRMALV AIMIFPVVLV
VMVIYQRYST PIVRRVRAYL ADINDGFNEI INGMSVIQQF RQQARFGERM GEASRSHYMA
RMQTLRLDGF LLRPLLSLFS SLILCGLLML FGFSASGTIE VGVLYAFISY LGRLNEPLIE
LTTQQAMLQQ AVVAGERVFE LMDGPRQQYG NDDRPLQSGT IEVDNVSFAY RDDNLVLKNI
NLSVPSRNFV ALVGHTGSGK STLASLLMGY YPLTEGEIRL DGRPLSSLSH SALRQGVAMV
QQDPVVLADT FLANVTLGRD ISEERVWQAL ETVQLAELAR SMSDGIYTPL GEQGNNLSVG
QKQLLALARV LVETPQILIL DEATASIDSG TEQAIQHALA AVREHTTLVV IAHRLSTIVD
ADTILVLHRG QAVEQGTHQQ LLAAQGRYWQ MYQLQLAGEE LAASVREEES LSA
