ID   MACB_CAMJE              Reviewed;         641 AA.
AC   Q0PAR0;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=Cj0607;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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       Confers resistance against macrolides. {ECO:0000255|HAMAP-
CC       Rule:MF_01720}.
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; AL111168; CAL34753.1; -; Genomic_DNA.
DR   PIR; F81408; F81408.
DR   RefSeq; WP_002858539.1; NC_002163.1.
DR   RefSeq; YP_002344037.1; NC_002163.1.
DR   AlphaFoldDB; Q0PAR0; -.
DR   SMR; Q0PAR0; -.
DR   IntAct; Q0PAR0; 4.
DR   STRING; 192222.Cj0607; -.
DR   PaxDb; Q0PAR0; -.
DR   PRIDE; Q0PAR0; -.
DR   EnsemblBacteria; CAL34753; CAL34753; Cj0607.
DR   GeneID; 904935; -.
DR   KEGG; cje:Cj0607; -.
DR   PATRIC; fig|192222.6.peg.599; -.
DR   eggNOG; COG0577; Bacteria.
DR   eggNOG; COG1136; Bacteria.
DR   HOGENOM; CLU_000604_78_2_7; -.
DR   OMA; VVILITH; -.
DR   Proteomes; UP000000799; 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; Reference proteome; Translocase;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..641
FT                   /note="Macrolide export ATP-binding/permease protein MacB"
FT                   /id="PRO_0000269933"
FT   TRANSMEM        265..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        519..539
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        571..591
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        604..624
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   DOMAIN          2..236
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   BINDING         34..41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ   SEQUENCE   641 AA;  70273 MW;  4F8CF6E1393C778B CRC64;
     MIFLKNICKN IGENAILKNV SLSIEKGEFV AIIGQSGSGK TSLLNIIGTL DTPSSGTYVF
     DEYEVTKLNN DEKARLRREK IGFIFQRYNL LSLLSAKENV SLPAVYAGKN LQERSQNAKK
     LLNDLELAHK LDSKPNELSG GQQQRVSIAR ALINGGELIL ADEPTGALDS KSGIMVLEIL
     QKLNEQGHTI VLVTHDPKIA AQAKRVIEIK DGEILSDTKK EKAQEKLILK TMPKEKKTLT
     LLKNQAFECF KIAYSSILAH KLRSILTMLG IIIGIASVVC VVALGLGSQA KVLESIARLG
     TNTIEIRPGK GFGDLRSGKT RLNFSDLETL RSLEYLEAVD AHSNTSGVAT YTNISLSARA
     EGVGVNNFAI EGLRIDAGRI LNNDDVKNST NVAVLDFNAK KNLFPDEKSE NILGRVVLFN
     SQPFKIIGVL QKDTDKPIED NVVRFYIPYT TLMNKLTGDR NLREIIVKVK DDVSSTLAEN
     AIIRILEIKR GQKDFFTFNS DTFKQAITAN KRTTTILTAC VAVIALIVGG IGVMNIMLVS
     VSERTREIGI RMAIGARRED IMMQFLIEAV MICTIGAILG VILSIFVIFA FNTLSTDFPM
     ILNAYSVLLG LLSSMFIGVV FGFFPARNAA NLNPISALSK E