MACB_AZOSB
ID MACB_AZOSB Reviewed; 656 AA.
AC A1K323;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=azo0611;
OS Azoarcus sp. (strain BH72).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=418699;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH72;
RX PubMed=17057704; DOI=10.1038/nbt1243;
RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT strain BH72.";
RL Nat. Biotechnol. 24:1385-1391(2006).
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; AM406670; CAL93228.1; -; Genomic_DNA.
DR RefSeq; WP_011764346.1; NC_008702.1.
DR AlphaFoldDB; A1K323; -.
DR SMR; A1K323; -.
DR STRING; 62928.azo0611; -.
DR EnsemblBacteria; CAL93228; CAL93228; azo0611.
DR KEGG; aoa:dqs_0680; -.
DR KEGG; azo:azo0611; -.
DR eggNOG; COG0577; Bacteria.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_78_2_4; -.
DR OMA; VVILITH; -.
DR OrthoDB; 1181903at2; -.
DR Proteomes; UP000002588; 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..656
FT /note="Macrolide export ATP-binding/permease protein MacB"
FT /id="PRO_0000280162"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 591..611
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 619..639
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT DOMAIN 20..258
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT BINDING 56..63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ SEQUENCE 656 AA; 69625 MW; A0096229CCF734E9 CRC64;
MKREAFSPSA SSTGAGTPLI ELAGITRSFR NGEIETRVLH GIDLTIYPGE FVAIVGASGS
GKSTLMNILG CLDRPSSGTY RFMGEDVAGF DRDELARLRR EAFGFVFQSY NLLGGASARE
NVEVPAVYSG MPPAERHARA EQLLASLGLG ERSHHRPSQL SGGQQQRVSI ARALMNGGRI
ILADEPTGAL DSRSGEEVMK LLRQLSAEGH TIILITHARE VAEMAQRIIE IRDGHIVADP
GPSKPQGPEP DFAPHVDRTS SMSDLVEATR TALRALRANL FRSALTLLGI VIGVASVIAM
LAIGDGAKAK VVDQISAMGT NLLTVRPGAP NQRGRETTAT LVIEDVRAIA ELPNVLASVP
EQSASVTLRA DNTDQRTTAN ATSWNYGVAR NWPVASGTFF SAEDEARYAT VAVLGQTTAG
ALFPGVDPIG QYVLVNNIPF QVIGVMSPKG ATPWGQDQDD IVFVPFTTGS LRVTGQRYLR
NVTVAVEDVS RIDATQNEVS QLLLARHGVE DFQIRNMASV IDTVSATQNT LTILLGTVAA
ISLLVGGIGV MNIMLVSVTE RTREIGIRMA TGARMKNILQ QFLIEALVVS ALGGLIGVAV
GLGTAAVIAL FDTPIKYSLL PVVLAFGCAF ATGLVFGYLP ARKAARLDPV VALASE