ID MACB_BORA1 Reviewed; 655 AA.
AC Q2KVS6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 99.
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=BAV2813;
OS Bordetella avium (strain 197N).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N;
RX PubMed=16885469; DOI=10.1128/jb.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ50424.1; -; Genomic_DNA.
DR RefSeq; WP_039051303.1; NC_010645.1.
DR AlphaFoldDB; Q2KVS6; -.
DR SMR; Q2KVS6; -.
DR STRING; 360910.BAV2813; -.
DR GeneID; 41394649; -.
DR KEGG; bav:BAV2813; -.
DR eggNOG; COG0577; Bacteria.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_78_2_4; -.
DR OrthoDB; 4814201at2; -.
DR Proteomes; UP000001977; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; P-loop containing nucleotide triphosphate hydrolases; 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-like_ATP-bd.
DR InterPro; IPR025857; MacB_PCD.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR30572:SF14; MACROLIDE EXPORT ATP-BINDING_PERMEASE PROTEIN MACB; 1.
DR PANTHER; PTHR30572; MEMBRANE COMPONENT OF TRANSPORTER-RELATED; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 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..655
FT /note="Macrolide export ATP-binding/permease protein MacB"
FT /id="PRO_0000269924"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 527..547
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 620..640
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 REGION 225..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ SEQUENCE 655 AA; 70536 MW; 4E7231FA662559F8 CRC64;
MSEPLIELRD VWREFAAGDQ VVAVLREVNL SIQAGEMVAI VGASGSGKST LMNILGCLDR
PSRGGYRVDG RETARMDPDE LAELRREHFG FIFQRYHLLA DLSAQANVEM PAVYAGMASG
PRHERAAALL RRLGLSERLD YRPGQLSGGQ QQRVSIARAL MNGGRIILAD EPTGALDTQT
GQEVLRILKE LNAAGHTIVL VTHDMSVARH ARRIIEISDG RIVSDQARPD APPLDALAGD
EGPEAPRPAP QPLRAWLDRG SEALRMALLA MNAHRLRTCL TMLGIIIGIA AVVSVVALGA
GSRQMILDDI SAMGTNTVDV LPGKHFGDEK AASIRTLVAA DVEALARQPY ADSVSPEVTT
SATLRYRNVS VNGTVQGVGE QYPRVRGVRI AQGQFFDAAA VARRGQDVVI DNNTRKALFG
NHTDPIGQVI FIGAVPARVI GVTRPQETLF GNADALHVWI PYTTALSRIL GQQHLRSITV
RVNDSTPPKA AEAAITKLML QRHGTQDFFV FNTDTIRQTV ERTTATLTLL VSMIAVISLV
VVGIGVMNIM LVSVTERTRE IGVRMAVGAR RSDIMQQFLI EAVLVCLIGG VLGILLSLSI
GVLVSQATRG AFQMLYSSGS MVLAFVCSTL IGVAFGFLPA RSAARLDPVE SLARE
//
