MACB_BDEBA
ID MACB_BDEBA Reviewed; 650 AA.
AC Q6MPX9;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=Bd0709;
OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS HD100).
OC Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC Bdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=264462;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX PubMed=14752164; DOI=10.1126/science.1093027;
RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA Schuster S.C.;
RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT genomic perspective.";
RL Science 303:689-692(2004).
CC -!- FUNCTION: Non-canonical ABC transporter that contains transmembrane
CC domains (TMD), which form a pore in the inner membrane, and an ATP-
CC binding domain (NBD), which is responsible for energy generation.
CC Confers resistance against macrolides. {ECO:0000255|HAMAP-
CC Rule:MF_01720}.
CC -!- SUBUNIT: Homodimer. {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; BX842647; CAE78668.1; -; Genomic_DNA.
DR RefSeq; WP_011163270.1; NC_005363.1.
DR AlphaFoldDB; Q6MPX9; -.
DR SMR; Q6MPX9; -.
DR STRING; 264462.Bd0709; -.
DR EnsemblBacteria; CAE78668; CAE78668; Bd0709.
DR KEGG; bba:Bd0709; -.
DR eggNOG; COG0577; Bacteria.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_78_2_7; -.
DR OMA; VVILITH; -.
DR OrthoDB; 1181903at2; -.
DR Proteomes; UP000008080; 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; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..650
FT /note="Macrolide export ATP-binding/permease protein MacB"
FT /id="PRO_0000269923"
FT TRANSMEM 267..287
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 580..600
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 610..630
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT DOMAIN 2..238
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ SEQUENCE 650 AA; 70886 MW; 2B7A78C4A4332867 CRC64;
MIDIKGIRKS YQMGDTKVDV LKGISLKIER GDFVAIMGPS GSGKSTLMHI LGLLDVPSEG
SYNLNGREVA DLSEDELAIV RREEIGFIFQ QFNLLPRMEA WQNVSLPLIY SEDGFSYDKA
QALLDKVGLA ERIHHKSNEL SGGQQQRIAI ARSLINNPRI IFADEPTGNL DSKSEKEIIQ
ILHKLNDQGI TVIVVTHEEE IGQQAKRLIR LRDGVIQSDE RLQALPAAPT TAQEKRQEKT
AKWPVREMIE HLHQGFQTLA ANKVRSGLSM LGILIGVAAV VGMLALGTGA RQSIEKQLSS
LGSNLLVLRA GNVRVGGVMQ ESGVRIRISL DDVSTIKNQI SGIKDVSPSS SGRGQITYLN
KNWNTQVMGV APAYEQMRAS TPIFGRFFSE EENQRRTLVA VIGTTVAREL FGEKSPIGEM
IKINKVNFRV IGVLPEKGAA GPQDQDDRIL VPVVTAMYRL FGRNYVDSVD IEVRDAADIP
EVQDSLQELM NKRHRVPVSS QGDAFNVFNM ADIQQALNST SQTLSMLLAS IAAISLVVGG
IGIMNIMLVS VTERTKEIGL RKAIGARRRD ILLQFLAESI VVSVCGGLLG IALGVGFSLL
ISKVLGWSTV VSAGSVILSF GFSALIGIVF GSYPASKASK LHPIEALRYE