ID   MACB1_ECOK1             Reviewed;         648 AA.
AC   A1A9B7;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, 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};
GN   OrderedLocusNames=Ecok1_07630; ORFNames=APECO1_1215;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
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; CP000468; ABJ00257.1; -; Genomic_DNA.
DR   RefSeq; WP_000188147.1; NC_008563.1.
DR   AlphaFoldDB; A1A9B7; -.
DR   SMR; A1A9B7; -.
DR   EnsemblBacteria; ABJ00257; ABJ00257; APECO1_1215.
DR   KEGG; ecv:APECO1_1215; -.
DR   HOGENOM; CLU_000604_78_2_6; -.
DR   OMA; VVILITH; -.
DR   Proteomes; UP000008216; 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                   1"
FT                   /id="PRO_0000280167"
FT   TRANSMEM        273..293
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        576..596
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;  70632 MW;  D0B55BABFF1652E8 CRC64;
     MTPLLELKDI RRSYPAGDEQ VEVLKGISLD IYAGEMVAIV GASGSGKSTL MNILGCLDKA
     TSGTYRVAGQ DVATLDADAL AQLRREHFGF IFQRYHLLSH LTAEQNVEVP AVYAGLERKQ
     RLLRAQELLQ RLGLEDRTEY YPAQLSGGQQ QRVSIARALM NGGQVILADE PTGALDSHSG
     EEVMAILHQL RDRGHTVIIV THDPQVAAQA ERVIEIRDGE IVRNPPAVEK VNATGGTEPV
     VNTASGWRQF VSGFNEALTM AWRALAANKM RTLLTMLGII IGIASVVSIV VVGDAAKQMV
     LADIRSIGTN TIDVYPGKDF GDDDPQYQQA LKYDDLIAIQ KQPWVASATP AVSQNLRLRY
     NNVDVAASAN GVSGDYFNVY GMTFSEGNTF NQEQLNGRAQ VVVLDSNTRR QLFPHKADVV
     GEVILVGNMP ARVIGVAEEK QSMFGSSKVL RVWLPYSTMS GRVMGQSWLN SITVRVKEGF
     DSAEAEQQLT RLLSLRHGKK DFFTWNMDGV LKTVEKTTRT LQLFLTLVAV ISLVVGGIGV
     MNIMLVSVTE RTREIGIRMA VGARASDVLQ QFLIEAVLVC LVGGALGITL SLLIAFTLQL
     FLPGWEIGFS PLALLLAFLC STVTGILFGW LPARNAARLD PVDALARE