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Database: UniProt
Entry: Q9K0N7
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ID   MACB_NEIMB              Reviewed;         644 AA.
AC   Q9K0N7;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 130.
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=NMB0549;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
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; AE002098; AAF40978.1; -; Genomic_DNA.
DR   PIR; C81187; C81187.
DR   RefSeq; NP_273594.1; NC_003112.2.
DR   RefSeq; WP_002247530.1; NC_003112.2.
DR   AlphaFoldDB; Q9K0N7; -.
DR   SMR; Q9K0N7; -.
DR   STRING; 122586.NMB0549; -.
DR   PaxDb; 122586-NMB0549; -.
DR   KEGG; nme:NMB0549; -.
DR   PATRIC; fig|122586.8.peg.699; -.
DR   HOGENOM; CLU_000604_78_1_4; -.
DR   InParanoid; Q9K0N7; -.
DR   OrthoDB; 4814201at2; -.
DR   Proteomes; UP000000425; 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: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..644
FT                   /note="Macrolide export ATP-binding/permease protein MacB"
FT                   /id="PRO_0000269950"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        524..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        574..594
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        607..627
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   DOMAIN          4..242
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ   SEQUENCE   644 AA;  69439 MW;  4256DC41D64D3A9D CRC64;
     MSLIECKNIN RYFGSGENRV HILKDISLSI EKGDFVAIIG QSGSGKSTLM NILGCLDTAG
     SGSYRIDGIE TAKMQPDELA ALRRERFGFI FQRYNLLSSL TARDNVALPA VYMGAGGKER
     SARADKLLQD LGLASKEGNK PGELSGGQQQ RVSIARALMN GGEIIFADEP TGALDTASGK
     NVMEIIRRLH EAGHTVIMVT HDPDIAANAN RVIEIRDGEI ISDTSKNPEI PASNVGRIRE
     KASWSFYYDQ FVEAFRMSVQ AVLAHKMRSL LTMLGIIIGI ASVVSVVALG NGSQKKILED
     ISSIGTNTIS IFPGRGFGDR RSGRIKTLTI DDAKIIAKQS YVASATPMTS SGGTLTYRNT
     DLTASLYGVG EQYFDVRGLK LETGRLFDEN DVKEDAQVVV IDQNVKDKLF ADSDPLGKTI
     LFRKRPLTVI GVMKKDENAF GNSDVLMLWS PYTTVMHQIT GESHTNSITV KIKDNANTQV
     AEKGLTDLLK ARHGTEDFFM NNSDSIRQIV ESTTGTMKLL ISSIALISLV VGGIGVMNIM
     LVSVTERTKE IGIRMAIGAR RGNILQQFLI EAVLICVIGG LVGVGLSAAV SLVFNHFVTD
     FPMDISAMSV IGAVACSTGI GIAFGFMPAN KAAKLNPIDA LAQD
//
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