ID MACB_CAMJR Reviewed; 641 AA.
AC Q5HVG3;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 115.
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=CJE0710;
OS Campylobacter jejuni (strain RM1221).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=195099;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM1221;
RX PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
RA Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
RA Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
RA Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
RA Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
RA Nelson K.E.;
RT "Major structural differences and novel potential virulence mechanisms from
RT the genomes of multiple Campylobacter species.";
RL PLoS Biol. 3:72-85(2005).
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; CP000025; AAW35780.1; -; Genomic_DNA.
DR RefSeq; WP_011049744.1; NC_003912.7.
DR AlphaFoldDB; Q5HVG3; -.
DR SMR; Q5HVG3; -.
DR KEGG; cjr:CJE0710; -.
DR HOGENOM; CLU_000604_78_2_7; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; P-loop containing nucleotide triphosphate hydrolases; 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-like_ATP-bd.
DR InterPro; IPR025857; MacB_PCD.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR30572:SF14; MACROLIDE EXPORT ATP-BINDING_PERMEASE PROTEIN MACB; 1.
DR PANTHER; PTHR30572; MEMBRANE COMPONENT OF TRANSPORTER-RELATED; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 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..641
FT /note="Macrolide export ATP-binding/permease protein MacB"
FT /id="PRO_0000269934"
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; 70229 MW; 35E91808605C71F0 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
SQSFKIIGVL QKDTDKPIED NVVRLYIPYT TLMNKLTGDR NLREIIVKVK DDVSSTLAEN
AIIRILEIKR GQKDFFTFNS DTFKQAITAN KRTTTILTAC VAVIALIVGG IGVMNIMLVS
VSERTREIGI RMAIGARRED IMMQFLIEAV MICTIGAILG VILSIFVIFA FNTLSTDFPM
ILNAYSVLLG LLSSMFIGVV FGFFPARNAA NLNPISALSK E
//
