ID   MDLB_BUCBP              Reviewed;         578 AA.
AC   Q89A96;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2003, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Multidrug resistance-like ATP-binding protein MdlB;
DE            EC=7.6.2.2;
GN   Name=mdlB; OrderedLocusNames=bbp_424;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC         xenobioticSide 2.; EC=7.6.2.2;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       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}.
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DR   EMBL; AE016826; AAO27134.1; -; Genomic_DNA.
DR   RefSeq; WP_011091535.1; NC_004545.1.
DR   AlphaFoldDB; Q89A96; -.
DR   SMR; Q89A96; -.
DR   STRING; 224915.bbp_424; -.
DR   EnsemblBacteria; AAO27134; AAO27134; bbp_424.
DR   GeneID; 56470959; -.
DR   KEGG; bab:bbp_424; -.
DR   eggNOG; COG1132; Bacteria.
DR   HOGENOM; CLU_000604_84_3_6; -.
DR   OMA; MSVMMAT; -.
DR   OrthoDB; 643917at2; -.
DR   Proteomes; UP000000601; 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; 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; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..578
FT                   /note="Multidrug resistance-like ATP-binding protein MdlB"
FT                   /id="PRO_0000092501"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        143..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          25..308
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          339..573
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         373..380
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   578 AA;  66827 MW;  3B84848CE196ADF7 CRC64;
     MNNVIDFWPT LKRLLYYGTN VKKYLILGFT LLLFSSIFEV LNPILISCFI KHYFINNTVN
     YSLKIITYYL ILQILAAILN YHQNIIFNKI SLTVIQKLRY DVMSSTLQLP IKMFDQRPIG
     QFISRITNDT ETIKELYDTV IKSLFQNIIL ILITLITMFI LEWRMACIAS IIFPIALIIM
     LLYQYFSKPI LRKIKVYIAN IYNIFNEIIN GIDVIQQFHQ EQKFRKSIKK ISISHYYFRM
     KILKLDSFLL RPLLNFCSTL ILCGLILIFG IYPIGFFEIG TLYAFITYLN RLNEPLITIT
     SQQSIFQQAI VAGERIFEII HTPKQQYGDD SLHFREGNIK VKNLYFSYTN NNVYVLKNIN
     IFIPSKQFIA FVGRTGSGKS TLSKLLIGHY PATLGKICLD ERNIQTFTHN VLKKNISIVQ
     QDPIILNDTI LENITLGRNI STKKVLKILK TIKLIQFVNS LPKGLKTLLG ENGNILSIGQ
     KQLLSIARTL ISCPKILILD EATSNVDLDT ENNIKKILSS VKHLTTIIAI THRLSTIKHA
     DNIFVFNNGE IVESGTHYNL IRKKSYYKNM YYSQAIKN