MACB_CAMFF
ID MACB_CAMFF Reviewed; 641 AA.
AC A0RP01;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
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};
GN OrderedLocusNames=CFF8240_0759;
OS Campylobacter fetus subsp. fetus (strain 82-40).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=82-40;
RA Fouts D.E., Nelson K.E.;
RT "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000487; ABK82901.1; -; Genomic_DNA.
DR RefSeq; WP_002849183.1; NC_008599.1.
DR AlphaFoldDB; A0RP01; -.
DR SMR; A0RP01; -.
DR STRING; 360106.CFF8240_0759; -.
DR PRIDE; A0RP01; -.
DR EnsemblBacteria; ABK82901; ABK82901; CFF8240_0759.
DR GeneID; 61064598; -.
DR KEGG; cff:CFF8240_0759; -.
DR PATRIC; fig|360106.6.peg.733; -.
DR eggNOG; COG0577; Bacteria.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_78_1_7; -.
DR OMA; NEIGVRM; -.
DR OrthoDB; 1181903at2; -.
DR Proteomes; UP000000760; 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..641
FT /note="Macrolide export ATP-binding/permease protein MacB"
FT /id="PRO_0000280164"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 601..621
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT DOMAIN 2..240
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ SEQUENCE 641 AA; 70007 MW; 9D724E789EC6EB5B CRC64;
MIKLENIKKS FITGGVSSEV LKGINLEIKK GEFVAIIGQS GSGKSTLMNI LGCLDTPTSG
KYLLDSLDIS KFKKDELSNL RLKKFGFIFQ RYNLLSSNDT KSNVALPGIY AGMSKADRIN
RAKDILVKLG LETKFDTMPN HLSGGQQQRV SIARALMNGG EILLCDEPTG ALDSSSGVMV
MQILDSLHKD GHTIIVVTHD KDIAAWADRI IEIKDGNIIS DTRKNSQIYE LKQNLKEIKP
SLKAIRDQFF ESFVMSLGAI KSHKLRSFLT MLGIIIGIAS VICVVALAKG SQQKILSDIN
NMGTNTITIF PGKGFGDMHS GRVRSLSIDD SNLLGKLDFV DFSTPRMNTS GLLTYANQSF
SGSLRSGSEY SLAISGLKIE KGRDFTKDDI INSRSNIIID QFTKDAFFKD VDPIGKVILF
NKQPFTIVGL VKRDETSFSG DNLTVYAPYT TTMNKLTGDR DIRSIMLKLK DGVNAQVAEQ
SIIEVLKIRR GSKDFFTRNS DTIRQTIEST MNTMSLLISG IALISLMVGG IGVMNIMLVS
VFERTKEIGI RMAIGAKSKD IMTQFLIEAI LLCAIGGSIG IGLAYAIGYG FNVFGGDFKM
IFSTASIFIA LGVSSLIGIV FGYIPARNAS KLNPIDALLR E