ID   MACB1_YERPA             Reviewed;         649 AA.
AC   Q1CA99;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Macrolide export ATP-binding/permease protein MacB 1 {ECO:0000255|HAMAP-Rule:MF_01720};
DE            EC=7.6.2.- {ECO:0000255|HAMAP-Rule:MF_01720};
GN   Name=macB1 {ECO:0000255|HAMAP-Rule:MF_01720}; OrderedLocusNames=YPA_0655;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- FUNCTION: Part of the tripartite efflux system MacAB-TolC. MacB is a
CC       non-canonical ABC transporter that contains transmembrane domains
CC       (TMD), which form a pore in the inner membrane, and an ATP-binding
CC       domain (NBD), which is responsible for energy generation. Confers
CC       resistance against macrolides. {ECO:0000255|HAMAP-Rule:MF_01720}.
CC   -!- SUBUNIT: Homodimer. Part of the tripartite efflux system MacAB-TolC,
CC       which is composed of an inner membrane transporter, MacB, a periplasmic
CC       membrane fusion protein, MacA, and an outer membrane component, TolC.
CC       The complex forms a large protein conduit and can translocate molecules
CC       across both the inner and outer membranes. Interacts with MacA.
CC       {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; CP000308; ABG12623.1; -; Genomic_DNA.
DR   RefSeq; WP_002211351.1; NZ_CP009906.1.
DR   AlphaFoldDB; Q1CA99; -.
DR   SMR; Q1CA99; -.
DR   EnsemblBacteria; ABG12623; ABG12623; YPA_0655.
DR   GeneID; 66842174; -.
DR   KEGG; ypa:YPA_0655; -.
DR   OMA; VVILITH; -.
DR   Proteomes; UP000001971; 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; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..649
FT                   /note="Macrolide export ATP-binding/permease protein MacB
FT                   1"
FT                   /id="PRO_0000269988"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        420..440
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        578..598
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        608..628
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   DOMAIN          5..243
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   BINDING         41..48
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ   SEQUENCE   649 AA;  70346 MW;  53762DD8C3924496 CRC64;
     MAALLELEGI RRSYQSGEEI VDVLQDVSLT INAGELVAII GASGSGKSTL MNILGCLDKP
     SAGIYRVAGQ NVDELDDDAL AALRREHFGF IFQRYHLLPH LSAAHNVEVP AVYAGLGKHE
     RRERANMLLT RLGLGDRVSY QPNQLSGGQQ QRVSIARALM NGGQVILADE PTGALDSHSS
     VEVMAILKQL QQQGHTVIIV THDPTVAAQA ERVIEIKDGR IMADSGSKNE PVVAAAELMS
     LTPAAPSWQQ LVGRFREALL MAWRAMSANK MRTALTMLGI IIGIASVVSI LVVGDAAKQL
     VLADIRAIGT NTIDIYPGKD FGDDDPSTRQ ALVHDDMAAL KAQSYVSAVS PSIGGSMRLR
     FGNIDVAASV LGVSDEYFRV FGMAMEQGAP ITREQVERQA QTVVIDLNTQ RRLFPHMKDV
     VGQVILVGNM PATVVGVVAE KKSMFGSNKA LRVWVPYSTM ANRLMGRSYF DSITIRIKEG
     YSSKEAEQQL VRLLTLRHGK KDIFTYNMDS LLQTAEKTTQ TMQLFLTLVA VISLVVGGIG
     VMNIMLVSVT ERTREIGIRM AVGARSSDVM QQFLIEAVLV CLIGGALGIS LSFAIGLIVE
     MFLPNWRIAF PPMALFSAFL CSTVIGVVFG YLPARSAARL NPIDALARE