ID   MACB2_ECOK1             Reviewed;         646 AA.
AC   P0C2H3; Q3L7H3;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Macrolide export ATP-binding/permease protein MacB 2 {ECO:0000255|HAMAP-Rule:MF_01720};
DE            EC=7.6.2.- {ECO:0000255|HAMAP-Rule:MF_01720};
GN   Name=macB2 {ECO:0000255|HAMAP-Rule:MF_01720}; Synonyms=etsB;
GN   OrderedLocusNames=Ecok1_ColBM_46970; ORFNames=O1_ColBM_198;
OS   Escherichia coli O1:K1 / APEC.
OG   Plasmid pAPEC-O1-ColBM.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885466; DOI=10.1128/jb.00204-06;
RA   Johnson T.J., Johnson S.J., Nolan L.K.;
RT   "Complete DNA sequence of a ColBM plasmid from avian pathogenic Escherichia
RT   coli suggests that it evolved from closely related ColV virulence
RT   plasmids.";
RL   J. Bacteriol. 188:5975-5983(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; DQ381420; ABD51768.1; -; Genomic_DNA.
DR   RefSeq; WP_000733250.1; NC_009837.1.
DR   AlphaFoldDB; P0C2H3; -.
DR   SMR; P0C2H3; -.
DR   EnsemblBacteria; ABD51768; ABD51768; APECO1_O1CoBM198.
DR   KEGG; ecv:APECO1_O1CoBM198; -.
DR   HOGENOM; CLU_000604_78_1_6; -.
DR   OMA; EGREHHK; -.
DR   Proteomes; UP000008216; Plasmid pAPEC-O1-ColBM.
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; Plasmid; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..646
FT                   /note="Macrolide export ATP-binding/permease protein MacB
FT                   2"
FT                   /id="PRO_0000278170"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        518..538
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        570..590
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   646 AA;  70385 MW;  01405822AC79BF5F CRC64;
     MKKLIELKGV SRTYGNGDQT RTVLKNVDLT IVAGEMVAII GASGSGKSTL MNIMGCLDVP
     NRGDYYIDGQ NAACLSPDEL ARVRREHIGF IFQRYHLIPD LSALGNVEIP AIYANSERDS
     RRQRATALLG RLGLEGREHH KPCELSGGQQ QRVSIARALI NGGKIILADE PTGALDSQSG
     QEVLAILNEL NRRGHTVVMV THDMKVARHA KRIIELCDGE IIADSGGCVS ATETLPKTNR
     IRQSYWKTLL DRTRESMQMA LKAMKTHRLR TTLTMIGIVF GIASVVTVVA LGEGARQETL
     EEIKSLGTNV VSIYPGQDLF DDSIESIRTL VPADANALAK QGFIDSVSPE VSASDNIRFL
     GKSAIASING VGREHFRVKG IELLQGTTFR DDRNALQEVI IDENTRKAIF DNTGLQALGQ
     IVFLGSVPAR VVGIAKSNNR SDASNRITVW MPYSTVMYRI VGKPVLTGIS VRLKDNVDNE
     AAISAISQLL TRRHGIKDFQ LYNFEQIRKS IEHTSMTFSI LILMVACISL MIGSIGVMNI
     MLISVTERTH EIGVRMAVGA RRSDIMQQFI IEAVLVCLIG GALGIALSYI TGALFNALAD
     GIFAAIYSWQ AAVAAFFCST LIGIIFGYLP ARKAARMDPV ISLASE