MACB_SODGM
ID MACB_SODGM Reviewed; 653 AA.
AC Q2NSZ1;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=SG1459;
OS Sodalis glossinidius (strain morsitans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=343509;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=morsitans;
RX PubMed=16365377; DOI=10.1101/gr.4106106;
RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA Aksoy S.;
RT "Massive genome erosion and functional adaptations provide insights into
RT the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL Genome Res. 16:149-156(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}.
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DR EMBL; AP008232; BAE74734.1; -; Genomic_DNA.
DR RefSeq; WP_011411279.1; NZ_LN854557.1.
DR AlphaFoldDB; Q2NSZ1; -.
DR SMR; Q2NSZ1; -.
DR STRING; 343509.SG1459; -.
DR PRIDE; Q2NSZ1; -.
DR EnsemblBacteria; BAE74734; BAE74734; SG1459.
DR KEGG; sgl:SG1459; -.
DR eggNOG; COG0577; Bacteria.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_78_2_6; -.
DR OMA; EGREHHK; -.
DR OrthoDB; 1181903at2; -.
DR BioCyc; SGLO343509:SGP1_RS12935-MON; -.
DR Proteomes; UP000001932; 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..653
FT /note="Macrolide export ATP-binding/permease protein MacB"
FT /id="PRO_0000269983"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 576..596
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 616..636
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 653 AA; 70588 MW; FA735928C2BFFD00 CRC64;
MTTPLIELQG VSRSYCQGDA TVNVLNDIHL RIDPGEMVAI IGSSGSGKST LMNILGCLDR
PSGGEYRIRG RDVAQLTPDA LAALRREHVG FIFQHYHLMP ELSAVGNVEI PAVYANRPRQ
ERRRRAAALL DRLGLAGKHH HCPAQLSGGQ QQRVSIARAL MNGGEIILAD EPTGALDSAS
GKEVLAILTE LNRQGHTLVI VTHDMAVARH ARRIIEIRDG RIVADTRTDQ TPLAPPLLPC
SAHPRRRRGA QFADRVRESL HMALKAMNAH RMRTLLTMAG IVFGIAAVVT VVGLGEGARE
QTLRRINFLG TNVISIYPGK DFFDENAGAI RTLVPADAVA LARQGYVDSV SPELGTSARL
RYRNKSANVD VIGVGESYFR VRGLSLAEGR TFTSQQVAQA TTDAIIDDNA RRTLFAATGQ
SPLGQTLLLN TMAVRVIGVA AADTNITGYH SDRIHIWLPY TTILHRLMGQ QHVNGIVVST
GAGIDNAAAE RTIEQLMLQR HGVKDFMLFN DDKIRRSVMK TSMTFSVLIT MVAMIALFIG
SLGVMNIMLV SVTERTHEIG VRMAVGARRG DIMQQFLIEA VLVCLTGGLL GVLLALSGGA
LFSALAGDIF PMVTSWPAVS GAFLCACAIG MVFGYWPARN AARLNPVEAL SSE