ID   LMRA_LACLA              Reviewed;         590 AA.
AC   Q9CHL8;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2003, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Multidrug resistance ABC transporter ATP-binding and permease protein;
DE            EC=7.6.2.2;
GN   Name=lmrA; OrderedLocusNames=LL0711; ORFNames=L116532;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
CC   -!- FUNCTION: Efflux transporter for a variety of amphiphilic cationic
CC       compounds, including antibiotics. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC         xenobioticSide 2.; EC=7.6.2.2;
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Multidrug
CC       exporter LmrA (TC 3.A.1.117.1) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK04809.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE005176; AAK04809.1; ALT_INIT; Genomic_DNA.
DR   PIR; G86713; G86713.
DR   RefSeq; NP_266867.1; NC_002662.1.
DR   PDB; 1MV5; X-ray; 3.10 A; A/B/C/D=349-590.
DR   PDBsum; 1MV5; -.
DR   AlphaFoldDB; Q9CHL8; -.
DR   SMR; Q9CHL8; -.
DR   STRING; 272623.L116532; -.
DR   PaxDb; Q9CHL8; -.
DR   EnsemblBacteria; AAK04809; AAK04809; L116532.
DR   KEGG; lla:L116532; -.
DR   PATRIC; fig|272623.7.peg.764; -.
DR   eggNOG; COG1132; Bacteria.
DR   HOGENOM; CLU_000604_84_3_9; -.
DR   OMA; ERQRMTI; -.
DR   EvolutionaryTrace; Q9CHL8; -.
DR   Proteomes; UP000002196; 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   GO; GO:0046677; P:response to antibiotic; 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   1: Evidence at protein level;
KW   3D-structure; Antibiotic resistance; ATP-binding; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..590
FT                   /note="Multidrug resistance ABC transporter ATP-binding and
FT                   permease protein"
FT                   /id="PRO_0000092413"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        292..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          38..317
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          349..584
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         382..389
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   STRAND          349..356
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   STRAND          358..362
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   STRAND          364..372
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   STRAND          376..381
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   HELIX           388..395
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   STRAND          402..404
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   STRAND          406..408
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   STRAND          411..413
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   TURN            414..416
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   TURN            422..424
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   HELIX           439..442
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   HELIX           453..463
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   TURN            466..470
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   HELIX           475..477
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   STRAND          479..481
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   HELIX           489..503
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   STRAND          506..511
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   STRAND          519..521
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   HELIX           524..533
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   STRAND          536..541
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   HELIX           545..550
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   STRAND          552..558
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   HELIX           568..574
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   HELIX           576..583
FT                   /evidence="ECO:0007829|PDB:1MV5"
FT   HELIX           584..588
FT                   /evidence="ECO:0007829|PDB:1MV5"
SQ   SEQUENCE   590 AA;  64698 MW;  8DF41419A01388CA CRC64;
     MERGPQMANR IEGKAVDKTS IKHFIKLIRA AKPRYLFFII GILAGIVGTL IQLQVPKMVQ
     PLVNSFGHGV NGGKVALVIA LYIGSAAVSA IAAIVLGIFG ESVVKNLRTR VWDKMIHLPV
     KYFDEVKTGE MSSRLANDTT QVKNLIANSI PQAFTSILLL VGSIVFMLQM QWRLTLAMII
     AVPVVMLIMF PIMTFGQKIG RTRQDSLANF QGIASESLSE IRLVKSSNAE KQASKKAEND
     VNALYKIGVK EAIFDGLMSP VMMLSMMLMI FGLLAYGIYL ISTGVMSLGT LLGMMMYLMN
     LIGAVPTVAT FFTELAKASG STGRLTELLD EEQEVLHQGE SLDLEGKTLS ARHVDFAYDD
     SEQILRDISF EAQPNSIIAF AGPSGGGKST IFSLLERFYQ PTAGEITIDG QPIDNISLEN
     WRSQIGFVSQ DSAIMAGTIR ENLTYGLEGD YTDEDLWQVL DLAFARSFVE NMPDQLNTEV
     GERGVKISGG QRQRLAIARA FLRNPKILML DEATASLDSE SESMVQKALD SLMKGRTTLV
     IAHRLSTIVD ADKIYFIEKG QITGSGKHNE LVATHPLYAK YVSEQLTVGQ