ID   MACB_NEIGO              Reviewed;         644 AA.
AC   Q5MK06;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
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};
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN MACROLIDE TRANSPORT.
RC   STRAIN=FA19;
RX   PubMed=16162665; DOI=10.1093/jac/dki333;
RA   Rouquette-Loughlin C.E., Balthazar J.T., Shafer W.M.;
RT   "Characterization of the MacA-MacB efflux system in Neisseria
RT   gonorrhoeae.";
RL   J. Antimicrob. Chemother. 56:856-860(2005).
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       Overexpression confers resistance against macrolides.
CC       {ECO:0000269|PubMed:16162665}.
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; AY768532; AAV85982.1; -; Genomic_DNA.
DR   RefSeq; WP_003689301.1; NZ_UGRM01000002.1.
DR   AlphaFoldDB; Q5MK06; -.
DR   SMR; Q5MK06; -.
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   1: Evidence at protein level;
KW   Antibiotic resistance; ATP-binding; Cell inner membrane; Cell membrane;
KW   Membrane; Nucleotide-binding; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..644
FT                   /note="Macrolide export ATP-binding/permease protein MacB"
FT                   /id="PRO_0000269947"
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;  69387 MW;  51038AE492B2200C CRC64;
     MSLIECKNIN RYFGSGENRV HILKDISLSI EKGDFVAIIG QSGSGKSTLM NILGCLDTAG
     SGSYRIDGIE TAKMQPDELA ALRRERFGFI FQRYNLLSSL TARDNVALPA VYMGMGGKER
     SARADKLLQD LGLASKEGNK PGELSGGQQQ RVSIARALMN GGEIIFADEP TGALDTASGK
     NVMEIIRRLH EAGHTVIMVT HDPGIAANAN RVIEIRDGEI ISDTSKNPEI PASNVGRIQE
     KASWSFYYDQ FVEAFRMSVQ AVLAHKMRSL LTMLGIIIGI ASVVSVVALG NGSQKKILED
     ISSMGTNTIS IFPGRGFGDR RSGKIKTLTI DDAKIIAKQS YVASATPMTS SGGTLTYRNT
     DLTASLYGVG EQYFDVRGLK LETGRLFDEN DVKEDAQVVV IDQNVKDKLF ADSDPLGKTI
     LFRKRPLTVI GVMKKDENAF GNSDVLMLWS PYTTVMHQIT GESHTNSITV KIKDNANTRV
     AEKGLAELLK ARHGTEDFFM NNSDSIRQMV ESTTGTMKLL ISSIALISLV VGGIGVMNIM
     LVSVTERTKE IGIRMAIGAR RGNILQQFLI EAVLICIIGG LVGVGLSAAV SLVFNHFVTD
     FPMDISAASV IGAVACSTGI GIAFGFMPAN KAAKLNPIDA LAQD