(data stored in ACNUC7421 zone)

SWISSPROT: MACB_ALCBS

ID   MACB_ALCBS              Reviewed;         644 AA.
AC   Q0VT01;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   11-DEC-2019, entry version 92.
DE   RecName: Full=Macrolide export ATP-binding/permease protein MacB {ECO:0000255|HAMAP-Rule:MF_01720};
DE            EC=7.6.2.- {ECO:0000255|HAMAP-Rule:MF_01720};
GN   Name=macB {ECO:0000255|HAMAP-Rule:MF_01720}; OrderedLocusNames=ABO_0249;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
CC   -!- FUNCTION: Part of the tripartite efflux system MacAB-TolC. MacB is a
CC       non-canonical ABC transporter that contains transmembrane domains
CC       (TMD), which form a pore in the inner membrane, and an ATP-binding
CC       domain (NBD), which is responsible for energy generation. Confers
CC       resistance against macrolides. {ECO:0000255|HAMAP-Rule:MF_01720}.
CC   -!- SUBUNIT: Homodimer. Part of the tripartite efflux system MacAB-TolC,
CC       which is composed of an inner membrane transporter, MacB, a periplasmic
CC       membrane fusion protein, MacA, and an outer membrane component, TolC.
CC       The complex forms a large protein conduit and can translocate molecules
CC       across both the inner and outer membranes. Interacts with MacA.
CC       {ECO:0000255|HAMAP-Rule:MF_01720}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01720}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01720}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Macrolide
CC       exporter (TC 3.A.1.122) family. {ECO:0000255|HAMAP-Rule:MF_01720}.
DR   EMBL; AM286690; CAL15697.1; -; Genomic_DNA.
DR   RefSeq; WP_011587545.1; NC_008260.1.
DR   SMR; Q0VT01; -.
DR   STRING; 393595.ABO_0249; -.
DR   EnsemblBacteria; CAL15697; CAL15697; ABO_0249.
DR   KEGG; abo:ABO_0249; -.
DR   eggNOG; ENOG4105D6C; Bacteria.
DR   eggNOG; COG0577; LUCA.
DR   eggNOG; COG1136; LUCA.
DR   HOGENOM; HOG000208217; -.
DR   KO; K05685; -.
DR   OMA; VVILITH; -.
DR   OrthoDB; 1181903at2; -.
DR   BioCyc; ABOR393595:ABO_RS01265-MONOMER; -.
DR   Proteomes; UP000008871; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0008559; F:ATPase-coupled xenobiotic transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015562; F:efflux transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IEA:UniProtKB-UniRule.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003838; ABC_permease_dom.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR017911; ABC_transptr_macrolide_ATP-bd.
DR   InterPro; IPR025857; MacB_PCD.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF02687; FtsX; 1.
DR   Pfam; PF12704; MacB_PCD; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51267; MACB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q0VT01.
DR   SWISS-2DPAGE; Q0VT01.
KW   Antibiotic resistance; ATP-binding; Cell inner membrane; Cell membrane;
KW   Membrane; Nucleotide-binding; Reference proteome; Translocase;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..644
FT                   /note="Macrolide export ATP-binding/permease protein MacB"
FT                   /id="PRO_0000269919"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        526..546
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        583..603
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        607..627
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   DOMAIN          4..242
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   NP_BIND         40..47
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ   SEQUENCE   644 AA;  68932 MW;  740E2082669763F2 CRC64;
     MPLIELCNIR KRYPAGDQDV EVLHGIDLSI EAGEFLAIMG SSGSGKSTLM HILGCLDQPS
     DGEYRFSGQP VTAMDHDQLA WLRREMFGFV FQSYHLIGTA SAWENVALPA IYAGVPREER
     KQRAQQLLTD LGLEDRLENR PSQLSGGQQQ RVSIARALMN GGKVILADEP TGALDSASGE
     AVMDQLRSLA EQGHTVIVIT HDAKVAAHAD RVVEIHDGNL ISDTRHHDHL HERAKPVSAP
     PKESVMPDPG EVMEAVVMAL RSLRANWMRT LLTLLGIVIG VGAVVVMLAI GEGAKQDVVA
     QINERGTNLL VVRPDRGMQR VADGVIATLV PADAQALESL PNISIAVPEI SGNVTARANG
     MDISTSVQAV SEDFPSLRDW QPVQGIFFGE EDLKSYSPVA VIGQTVKENL FPEGDPLGQF
     LLLDSIPFQV IGVMSAQGAS DRGEDQDDVV IVPLSTGTLR LFGQNYLNSI TVAVDDVTQI
     DATEAAAVAL LTQRHGKQDV RVFNMASLLE MVSETQNTLT ALLGSIAAIS LLVGGIGVMN
     IMLVSVTERI HEIGIRMATG ARQRNILQQF LTESVVVSAL GGIVGVVIGV LVGWLLMLFG
     MAIVFSVPVM VVSFVCAAGI GLLFGFAPAL KAARLNPVEA LSND
//

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