MACB_AROAE
ID MACB_AROAE Reviewed; 641 AA.
AC Q5P6D5;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, 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=AZOSEA10010;
GN ORFNames=ebA1848;
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1;
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI07126.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR555306; CAI07126.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q5P6D5; -.
DR SMR; Q5P6D5; -.
DR STRING; 76114.ebA1848; -.
DR EnsemblBacteria; CAI07126; CAI07126; ebA1848.
DR KEGG; eba:ebA1848; -.
DR eggNOG; COG0577; Bacteria.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_78_2_4; -.
DR OMA; VVILITH; -.
DR Proteomes; UP000006552; 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_0000269920"
FT TRANSMEM 267..287
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 573..593
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 4..242
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ SEQUENCE 641 AA; 67786 MW; ECD6710C803537A6 CRC64;
MPLIELSGVT KTFRNGELAV EVLHGIDLTI LPGEFVAIVG SSGSGKSTLM NILGCLDRPT
SGSYRFMGRN VAAFDRDELA LLRRETFGFV FQSYHLIGGA SARENVEVPA VYSGMPPAER
HARATGLLAS LGLGERIEHR PNQLSGGQQQ RVSIARALMN GGRVILADEP TGALDTKSGA
EVMQLLNKLS ADGHTIILIT HEREVAEQAQ RIIEIRDGRI VADPGPRPRS GLEPDFAPHV
DRTSPLSDIV EAARTALRAL RANIFRAALT LLGIVIGVAA VIAMLAIGDG AKQDVVDRIS
SMGTNLLTVR PGAPNQRGRD TTATLVLDDV RAIRDLPNVL AAVPEQSSTV TIRSGNADHR
TSANATGADF TLARAWPIAR GTFFGAADER SYATVAVLGQ TVAKALFGDA DPVGEFVLVN
SIMFQVLGVM GPQGATPWGT DQDDVIFVPY STGSLRLFGQ RHLRNATIAV EDVAAIDDTQ
AAVHELLQAR HGGIEDFQIR NMASVIESVS ETQNTLTVLL GTVAAISLLV GGIGVMNIML
VSVTERTREI GIRMATGARM KNILQQFLIE ALVVSALGGV IGVVVGLGAA AIIEAFDTPI
VYSAPPVLLA FGCAFATGLV FGYLPARKAA RLDPVVALAS E