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Database: UniProt
Entry: Q7ULB5
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Original site: Q7ULB5 
ID   MACB_RHOBA              Reviewed;         684 AA.
AC   Q7ULB5;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 119.
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=RB9611;
OS   Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Rhodopirellula.
OX   NCBI_TaxID=243090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX   PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA   Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA   Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA   Reinhardt R.;
RT   "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT   1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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; BX294149; CAD76362.1; -; Genomic_DNA.
DR   RefSeq; NP_868977.1; NC_005027.1.
DR   RefSeq; WP_011122387.1; NC_005027.1.
DR   AlphaFoldDB; Q7ULB5; -.
DR   SMR; Q7ULB5; -.
DR   STRING; 243090.RB9611; -.
DR   EnsemblBacteria; CAD76362; CAD76362; RB9611.
DR   KEGG; rba:RB9611; -.
DR   PATRIC; fig|243090.15.peg.4615; -.
DR   eggNOG; COG0577; Bacteria.
DR   eggNOG; COG1136; Bacteria.
DR   HOGENOM; CLU_000604_78_2_0; -.
DR   InParanoid; Q7ULB5; -.
DR   OrthoDB; 9770099at2; -.
DR   Proteomes; UP000001025; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
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:SF4; 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..684
FT                   /note="Macrolide export ATP-binding/permease protein MacB"
FT                   /id="PRO_0000269970"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        563..583
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        615..635
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        644..664
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   DOMAIN          2..243
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   684 AA;  73964 MW;  D9EAFE8C726D5087 CRC64;
     MIQLYGLRKD YRVGDHDLPV LKGITLNIEA GEYVALMGSS GSGKTTLMNL LGSLDHPTDG
     DYHLAGIDVS SLTPLELAAF RSQHIGFVFQ NFNLLPRATA LDNVMLPTIY ASDGRSRREC
     IEDATKLLES VGLGGRLDHM PNQLSGGERQ RIAIARALMN RPKLLLADEP TGNLDTVTEQ
     EILALFRQLN QEHGITLVVV THDAEVAHEA DRVVRMKDGL VAEDVRQRAS TVDRSRLANS
     RAEPLREPAS AWSLPATWNA IVVAVLALRR NALRTVLTML GVIIGVASVI STMELSAGAS
     TAIEETVASM GASMLTISPG KASSTSGRQR PIQIIPDDVV AVAEQCSAVK VAAPLVYSQV
     QLVRQNRRWS PNLALGTTSQ YLAARNWDQL ELGTPFTQEQ VLDAAKVCIL GKTVAHELFD
     SEYPIGEEIR VNGVPLRVVG VLTEKGGDVI GNDQDDIIIG PWTTFKLRVN SSTGATAQFS
     TFADQMPPMQ LASTRRSTQR EEIHQIYVEA ESPDHVELAR QQITQVLSRR HNVEPAGAYR
     INDITEVSKV VGQVVGGVSA LGLVIAGVSL MVGGVGIMNI MLVSVTERTR EIGLRMAVGA
     NRSAILRQFL IEATVLCVVG GFIGIFAGHM WSVLVGRVIG WPTAMSIWAP IVAVTVAATV
     GIVFGYYPAR TASRLNPIDA LRYE
//
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