MACB_NITWN
ID MACB_NITWN Reviewed; 645 AA.
AC Q3SQZ1;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=Nwi_2041;
OS Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 /
OS NCIMB 11846 / Nb-255).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Nitrobacter.
OX NCBI_TaxID=323098;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255;
RX PubMed=16517654; DOI=10.1128/aem.72.3.2050-2063.2006;
RA Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L.,
RA Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J.,
RA Hickey W.J.;
RT "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium
RT Nitrobacter winogradskyi Nb-255.";
RL Appl. Environ. Microbiol. 72:2050-2063(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; CP000115; ABA05300.1; -; Genomic_DNA.
DR RefSeq; WP_011315283.1; NC_007406.1.
DR AlphaFoldDB; Q3SQZ1; -.
DR SMR; Q3SQZ1; -.
DR STRING; 323098.Nwi_2041; -.
DR EnsemblBacteria; ABA05300; ABA05300; Nwi_2041.
DR KEGG; nwi:Nwi_2041; -.
DR eggNOG; COG0577; Bacteria.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_78_2_5; -.
DR OMA; VVILITH; -.
DR OrthoDB; 1181903at2; -.
DR Proteomes; UP000002531; 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..645
FT /note="Macrolide export ATP-binding/permease protein MacB"
FT /id="PRO_0000269951"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 574..594
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 596..616
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT DOMAIN 6..244
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ SEQUENCE 645 AA; 68174 MW; D9DA94967BE26A3D CRC64;
MTPPLIELEG IRRSYRSGDV VTHALRGVGL SIHAGEFVAI IGASGSGKST LMNIIGLMDR
PSDGAYRFGG RDVATLNRDE LAALRRGCFG FIFQNYHLIP TVSALGNVEM PAIHAGAPRA
YRHRRATALL TRLGLANRIT NRPSQLSGGQ QQRVSIARAL MNGGAVILAD EPTGALDSKS
GTEVLGILKK LAGDGHTVIL ITHDSKVAAA AERIIRIEDG LIVSDSGPDP EKVSSSIAVV
PWQASDSSPP LWTWLEEAAR SAFAALAINP VRTALTLSGI VIGVASVVAM MAIGRGAQAS
YIERASAIGT NWIVVDRAGE STGNSLPLTP ADAQAIKDMD NVSGSMPAMW DMATMRRGNI
DLNTDVVATT AEFRTVHNWD MAKGTFFTKQ DEVSGGPVVL LGATLASKLF PGIADPSGSN
ILINNLPFLV TGVLESKGLS ERGTDRDKRA VMPLRTATMR LFGKDDLSEI VVSIADMSRL
HETKEAIKAL LIRRHGREDF YIYDSASAFQ KAEDERRSSN LLLSAIAAIS MLVGGIGIMN
IMLITVSERT REIGVRTAIG ARTADILGQF LTEAVVLAAI GGVVGLLLGA VIGVGAALLF
GMTVIFSVTM ALGALMGAVV MGTVFGFMPA YRAARLKPIE ALARG