MDLB_ECOLI
ID MDLB_ECOLI Reviewed; 593 AA.
AC P0AAG5; P30751; P75706; P77117; Q2MBX7;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Multidrug resistance-like ATP-binding protein MdlB;
DE EC=7.6.2.2;
GN Name=mdlB; Synonyms=mdl; OrderedLocusNames=b0449, JW5061;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TAP90 / ATCC 47037;
RX PubMed=7904973; DOI=10.1016/0378-1119(93)90470-n;
RA Allikmets R., Gerrard B.C., Court D., Dean M.C.;
RT "Cloning and organization of the abc and mdl genes of Escherichia coli:
RT relationship to eukaryotic multidrug resistance.";
RL Gene 136:231-236(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Drug exporter-2
CC (TC 3.A.1.117) family. {ECO:0000305}.
CC -!- CAUTION: Was originally proposed to be fused with MdlA.
CC {ECO:0000305|PubMed:7904973}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40205.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAC36870.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L08627; AAC36870.1; ALT_INIT; Unassigned_DNA.
DR EMBL; U82664; AAB40205.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73552.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76229.1; -; Genomic_DNA.
DR PIR; A64775; A64775.
DR RefSeq; NP_414983.1; NC_000913.3.
DR RefSeq; WP_001256201.1; NZ_SSZK01000009.1.
DR AlphaFoldDB; P0AAG5; -.
DR SMR; P0AAG5; -.
DR BioGRID; 4261405; 185.
DR STRING; 511145.b0449; -.
DR TCDB; 3.A.1.106.13; the atp-binding cassette (abc) superfamily.
DR PaxDb; P0AAG5; -.
DR PRIDE; P0AAG5; -.
DR EnsemblBacteria; AAC73552; AAC73552; b0449.
DR EnsemblBacteria; BAE76229; BAE76229; BAE76229.
DR GeneID; 945088; -.
DR KEGG; ecj:JW5061; -.
DR KEGG; eco:b0449; -.
DR PATRIC; fig|1411691.4.peg.1827; -.
DR EchoBASE; EB4117; -.
DR eggNOG; COG1132; Bacteria.
DR HOGENOM; CLU_000604_84_3_6; -.
DR InParanoid; P0AAG5; -.
DR OMA; MSVMMAT; -.
DR PhylomeDB; P0AAG5; -.
DR BioCyc; EcoCyc:MDLB-MON; -.
DR PRO; PR:P0AAG5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..593
FT /note="Multidrug resistance-like ATP-binding protein MdlB"
FT /id="PRO_0000092496"
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"
FT CONFLICT 208..209
FT /note="NE -> KQ (in Ref. 1; AAC36870)"
FT /evidence="ECO:0000305"
FT CONFLICT 336..337
FT /note="LQ -> FT (in Ref. 1; AAC36870)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="K -> N (in Ref. 1; AAC36870)"
FT /evidence="ECO:0000305"
FT CONFLICT 411..414
FT /note="SALR -> TRG (in Ref. 1; AAC36870)"
FT /evidence="ECO:0000305"
FT CONFLICT 457..458
FT /note="EL -> DV (in Ref. 1; AAC36870)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="D -> A (in Ref. 1; AAC36870)"
FT /evidence="ECO:0000305"
FT CONFLICT 563..593
FT /note="AAQGRYWQMYQLQLAGEELAASVREEESLSA -> RPRDVLADVSTATCGRR
FT AGSQRA (in Ref. 1; AAC36870)"
FT /evidence="ECO:0000305"
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
