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MACB_SHESA
ID   MACB_SHESA              Reviewed;         656 AA.
AC   A0L0V9;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
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};
GN   OrderedLocusNames=Shewana3_3455;
OS   Shewanella sp. (strain ANA-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=94122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANA-3;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA   Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000469; ABK49678.1; -; Genomic_DNA.
DR   RefSeq; WP_011718247.1; NC_008577.1.
DR   AlphaFoldDB; A0L0V9; -.
DR   SMR; A0L0V9; -.
DR   STRING; 94122.Shewana3_3455; -.
DR   EnsemblBacteria; ABK49678; ABK49678; Shewana3_3455.
DR   KEGG; shn:Shewana3_3455; -.
DR   eggNOG; COG0577; Bacteria.
DR   eggNOG; COG1136; Bacteria.
DR   HOGENOM; CLU_000604_78_1_6; -.
DR   OMA; NEIGVRM; -.
DR   OrthoDB; 1181903at2; -.
DR   Proteomes; UP000002589; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   CDD; cd03255; ABC_MJ0796_LolCDE_FtsE; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003838; ABC3_permease_dom.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR017911; MacB_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;
KW   Antibiotic resistance; ATP-binding; Cell inner membrane; Cell membrane;
KW   Membrane; Nucleotide-binding; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..656
FT                   /note="Macrolide export ATP-binding/permease protein MacB"
FT                   /id="PRO_0000280174"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        531..551
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        586..606
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        621..641
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   DOMAIN          6..244
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   BINDING         42..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ   SEQUENCE   656 AA;  70578 MW;  391D4167BF42C31C CRC64;
     MSKPLLEVSA CYRSFQAGEQ QLTVLKDINL SIARGEMVAI VGASGSGKST LMNILGCLDK
     PSKGSYFIDG QDTSQMDVDE LAKLRREHFG FIFQRYHLLG DLNAVGNVEV PAVYAGKDRL
     ERRERAESLL SRLGLGERLD HKPNQLSGGQ QQRVSVARAL MNGGDVILAD EPTGALDSHS
     GEEMMRLLQE LHREGQTIII VTHDMHVAQH ADRIIEIKDG VIISDEPNPA SNIAAAPKTE
     VIPAKTKARA RVAAWDRYAE ALKMALLAMS THRLRTFLTM LGIIIGIASV VSVVALGEGS
     QREILKSISS MGTNTIDIRP GSGFGDRRSA RVRTLTASDA NALKNLPYVD SVTPSIGSSA
     TVRYGNKAVT ATVNGVGPEF FRVRGYELAQ GQFWDDDSVN ALAQDAVIDE NTRKQLFPNS
     SGAMNSAIGE VIFLGDLPVR IIGVTQPKES AFGNSDALNV WVPYTTVSGR MVGKKYLDGI
     TVRLDESVPS NAAEQGIISL LKMRHGTQDF FTINTDTIRQ NIEKTTATMT LLISAIAVIS
     LVVGGIGVMN IMLVSVTERT REIGVRMAVG ARQSDILRQF LIEAVLVCLC GGALGVALAY
     LIGVVFAQAG GSFQMIYSTT SIVAAFACST LIGVLFGFLP ARNAARLDPV DALARE
 
 
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