MACB_NITEU
ID MACB_NITEU Reviewed; 659 AA.
AC Q82VK1;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=NE1081;
OS Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC
OS 14298).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=228410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298;
RX PubMed=12700255; DOI=10.1128/jb.185.9.2759-2773.2003;
RA Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT "Complete genome sequence of the ammonia-oxidizing bacterium and obligate
RT chemolithoautotroph Nitrosomonas europaea.";
RL J. Bacteriol. 185:2759-2773(2003).
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; AL954747; CAD84992.1; -; Genomic_DNA.
DR RefSeq; WP_011111680.1; NC_004757.1.
DR AlphaFoldDB; Q82VK1; -.
DR SMR; Q82VK1; -.
DR STRING; 228410.NE1081; -.
DR EnsemblBacteria; CAD84992; CAD84992; NE1081.
DR KEGG; neu:NE1081; -.
DR eggNOG; COG0577; Bacteria.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_78_2_4; -.
DR OMA; VVILITH; -.
DR OrthoDB; 1181903at2; -.
DR PhylomeDB; Q82VK1; -.
DR Proteomes; UP000001416; 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..659
FT /note="Macrolide export ATP-binding/permease protein MacB"
FT /id="PRO_0000269952"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 538..558
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 594..614
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 10..249
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT BINDING 47..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ SEQUENCE 659 AA; 72075 MW; 5A591DE060CA4E0D CRC64;
MVSTDLPPLI ELRGIRKRYG GGDKPEVEVL HGIDLDIRAG EFIAIVGSSG SGKSTLMHLL
GCLDRPSSGS YRFAGEDVST FGSDELAWLR RKAFGFVFQG YHLIPTESAR ENVEIPAIYA
GLPPGERMQR AADLLGRLGL SDKLNNRPNQ LSGGQQQRVS IARALMNGGH IILADEPTGA
LDSRSGAEVM ELLRELAGAG HTVILITHDR DVAAQAQRVV EIRDGRIVAD SVTDRQPSEQ
PLLHHAGLSS LEMTQAHEDT GTPFWQGLHE TIRAAWRVMW IHRVRTSLTL LGIVIGVASV
IVMLAIGEGT KQRVIDQMGS MGTTIMYMSS DVPSTGGPVG VITEEDLDEV ARLPEISRVM
PVIGDPILVR HQNVDKQIYV FSSPYIMPMV HHWRVAQGRF FTETEDRELA PVVVLGHKIY
RSFFPHLSNP VGQYLLIGTS PFEVIGVMAE RGAESGSQNY DDMVFIPYRA GRARVYQAQE
QPDYIVMEAA SMDQVQEAEE AIRALLLERH GREDFRIGNA AARLKTQLET RDTMTRMLGL
VAAVSLLVGG IGVMNVMLMT VRERTREIGI RMATGAREYD ILSQFLIEAM LVTITGGTVG
VILGLTVGAL LVFWEVPVVF SFGVMIGAFA CAVITGLIFG YMPARTAARL DPVVALSSE