ID   MACB_SALCH              Reviewed;         648 AA.
AC   Q57R58;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=SCH_0897;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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; AE017220; AAX64803.1; -; Genomic_DNA.
DR   RefSeq; WP_000125882.1; NC_006905.1.
DR   AlphaFoldDB; Q57R58; -.
DR   SMR; Q57R58; -.
DR   EnsemblBacteria; AAX64803; AAX64803; SCH_0897.
DR   KEGG; sec:SCH_0897; -.
DR   HOGENOM; CLU_000604_78_3_6; -.
DR   OMA; VVILITH; -.
DR   Proteomes; UP000000538; 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..648
FT                   /note="Macrolide export ATP-binding/permease protein MacB"
FT                   /id="PRO_0000269974"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        417..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        523..543
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        577..597
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        611..631
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   648 AA;  70799 MW;  E1C74B20D3ED0849 CRC64;
     MTALLELCNV SRSYPSGEEQ VAVLKDISLQ IHAGEMVAIV GVSGSGKSTL MNILGCLDKP
     TSGTYRVAGR DVSTLDPDAL AQLRREHFGF IFQRYHLLSH LTAAQNVEIP AVYAGIERKK
     RQTRARELLL RLGLSDRVDY PPSQLSGGQQ QRVSIARALM NGGQVILADE PTGALDSHSG
     EEVMAILRQL RDRGHTVIIV THDPLIAAQA ERIIEIHDGK IVHNPPAQEK KREQGVDAAV
     VNTAPGWRQF ASSFREALSM AWLAMAANKM RTLLTMLGII IGIASVVSIV VVGDAAKQMV
     LADIRAMGTN TIDIHPGKDF GDDNPQYRQA LKYDDLVAIQ KQPWVNSATP SVSKSLRLRY
     GNIDIAVNAN GVSGDYFNVY GMSFREGNTF NAVQQQDRAQ VVVLDANTRR QLFPNKANVV
     GEVVLAGNMP VIVIGVAEEK PSMYGNSNLL QVWLPYSTMS DRIMGQSWLN SITVRVKDGV
     DSDQAEQQLT RLLTLRHGKK DFFTWNMDSV LKTAEKTTYT LQLFLTLVAV ISLVVGGIGV
     MNIMLVSVTE RTREIGIRMA VGARASDVLQ QFLIEAVLVC LVGGALGISL SMFIAFMLQL
     FLPGWEIGFS LTALASAFLC STFTGILFGW LPARNAARLD PVDALARE