MDLA_BUCAP
ID MDLA_BUCAP Reviewed; 581 AA.
AC Q8K985;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Multidrug resistance-like ATP-binding protein MdlA;
DE EC=7.6.2.2;
GN Name=mdlA; OrderedLocusNames=BUsg_464;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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}.
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; AE013218; AAM68007.1; -; Genomic_DNA.
DR RefSeq; WP_011053974.1; NC_004061.1.
DR AlphaFoldDB; Q8K985; -.
DR SMR; Q8K985; -.
DR STRING; 198804.BUsg_464; -.
DR EnsemblBacteria; AAM68007; AAM68007; BUsg_464.
DR KEGG; bas:BUsg_464; -.
DR eggNOG; COG1132; Bacteria.
DR HOGENOM; CLU_000604_84_3_6; -.
DR OMA; RVMHDLR; -.
DR OrthoDB; 643917at2; -.
DR Proteomes; UP000000416; 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 membrane; Membrane; Nucleotide-binding; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..581
FT /note="Multidrug resistance-like ATP-binding protein MdlA"
FT /id="PRO_0000092494"
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 127..149
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 153..175
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 247..267
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..571
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"
SQ SEQUENCE 581 AA; 66160 MW; 004B5AC7FE5A7B96 CRC64;
MRLFNQLKWY FIKEWKRYLG SIILLIIIAF LQLLPPKIIG ILIDLIIKEK MSGFEILPWI
SIILLIAIIV YILRYLWRIL LFGASYQLAT ELRVKFYSYL SKQSEIFFLK NRTGDLIARA
TNDVDRVVFA AGEGVLTLVD SSVMGISVLI VMITQISWLL TIISLIPMPI MAILIKKYGK
KLHDTFRNAQ SAFSLLNNQT QEILTSIRMI RAFGLEKNQL KKFNNIVNDT GKKNMEVAEI
DARFDPVIYL SVAFSNLLAI TAGGWLVWNN TITIGKLTSF IMYLGLMIWP MLALAWMFNI
VERGSAAWDR IHSIINQNLY IEDGKKTIIN MNGKLNINID MFFYPKNKKP SLKNIYLSLN
PGKTLGICGP TGAGKSTLLK LIQRQFKIHK GEILYNSSSL LELKIDYWRS KIGVVNQTSF
LFSDSISNNI SLGKPKASQK EIEKAAKLAD IHKDIVCLPQ GYNTQVGERG VMLSGGQKQR
IAIARALLLN TEILILDDAL SAVDGKTENN ILKNLKKWKD KGYSLIIVAH RLSALIHADE
IIVIKEGTII QRGNHEKLIK EKNWYKSMYD HQKIQTEIEN F