MDLA_ECOLI
ID MDLA_ECOLI Reviewed; 590 AA.
AC P77265; P30751; Q2MBX8;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Multidrug resistance-like ATP-binding protein MdlA;
DE EC=7.6.2.2;
GN Name=mdlA; Synonyms=mdl; OrderedLocusNames=b0448, JW0438;
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 SUBCELLULAR LOCATION.
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
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:15919996}.
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=AAC36870.1; Type=Frameshift; Note=Fuses together mdlA and mdlB.; Evidence={ECO:0000305};
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DR EMBL; L08627; AAC36870.1; ALT_FRAME; Unassigned_DNA.
DR EMBL; U82664; AAB40204.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73551.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76228.1; -; Genomic_DNA.
DR PIR; H64774; H64774.
DR RefSeq; NP_414982.1; NC_000913.3.
DR RefSeq; WP_001235649.1; NZ_SSZK01000009.1.
DR AlphaFoldDB; P77265; -.
DR SMR; P77265; -.
DR BioGRID; 4261677; 157.
DR DIP; DIP-10173N; -.
DR IntAct; P77265; 1.
DR STRING; 511145.b0448; -.
DR TCDB; 3.A.1.106.13; the atp-binding cassette (abc) superfamily.
DR PaxDb; P77265; -.
DR PRIDE; P77265; -.
DR EnsemblBacteria; AAC73551; AAC73551; b0448.
DR EnsemblBacteria; BAE76228; BAE76228; BAE76228.
DR GeneID; 945092; -.
DR KEGG; ecj:JW0438; -.
DR KEGG; eco:b0448; -.
DR PATRIC; fig|1411691.4.peg.1828; -.
DR EchoBASE; EB1579; -.
DR eggNOG; COG1132; Bacteria.
DR HOGENOM; CLU_000604_84_6_6; -.
DR InParanoid; P77265; -.
DR OMA; RVMHDLR; -.
DR PhylomeDB; P77265; -.
DR BioCyc; EcoCyc:MDLA-MON; -.
DR PRO; PR:P77265; -.
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 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..590
FT /note="Multidrug resistance-like ATP-binding protein MdlA"
FT /id="PRO_0000092492"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 18..303
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 337..570
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 369..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 145
FT /note="G -> A (in Ref. 1; AAC36870)"
FT /evidence="ECO:0000305"
FT CONFLICT 234..235
FT /note="NM -> KL (in Ref. 1; AAC36870)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="A -> R (in Ref. 1; AAC36870)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="T -> N (in Ref. 1; AAC36870)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="E -> P (in Ref. 1; AAC36870)"
FT /evidence="ECO:0000305"
FT CONFLICT 410..411
FT /note="SR -> TG (in Ref. 1; AAC36870)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 590 AA; 66017 MW; AD1CEBE41030200D CRC64;
MRLFAQLSWY FRREWRRYLG AVALLVIIAM LQLVPPKVVG IVVDGVTEQH FTTGQILMWI
ATMVLIAVVV YLLRYVWRVL LFGASYQLAV ELREDYYRQL SRQHPEFYLR HRTGDLMARA
TNDVDRVVFA AGEGVLTLVD SLVMGCAVLI MMSTQISWQL TLFSLLPMPV MAIMIKRNGD
ALHERFKLAQ AAFSSLNDRT QESLTSIRMI KAFGLEDRQS ALFAADAEDT GKKNMRVARI
DARFDPTIYI AIGMANLLAI GGGSWMVVQG SLTLGQLTSF MMYLGLMIWP MLALAWMFNI
VERGSAAYSR IRAMLAEAPV VNDGSEPVPE GRGELDVNIH QFTYPQTDHP ALENVNFALK
PGQMLGICGP TGSGKSTLLS LIQRHFDVSE GDIRFHDIPL TKLQLDSWRS RLAVVSQTPF
LFSDTVANNI ALGCPNATQQ EIEHVARLAS VHDDILRLPQ GYDTEVGERG VMLSGGQKQR
ISIARALLVN AEILILDDAL SAVDGRTEHQ ILHNLRQWGQ GRTVIISAHR LSALTEASEI
IVMQHGHIAQ RGNHDVLAQQ SGWYRDMYRY QQLEAALDDA PENREEAVDA
