MACB_RHOPB
ID MACB_RHOPB Reviewed; 655 AA.
AC Q217L2;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=RPC_1867;
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-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; CP000301; ABD87424.1; -; Genomic_DNA.
DR RefSeq; WP_011472328.1; NC_007925.1.
DR AlphaFoldDB; Q217L2; -.
DR SMR; Q217L2; -.
DR STRING; 316056.RPC_1867; -.
DR EnsemblBacteria; ABD87424; ABD87424; RPC_1867.
DR KEGG; rpc:RPC_1867; -.
DR eggNOG; COG0577; Bacteria.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_78_1_5; -.
DR OMA; NEIGVRM; -.
DR OrthoDB; 1181903at2; -.
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..655
FT /note="Macrolide export ATP-binding/permease protein MacB"
FT /id="PRO_0000269971"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 579..599
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 618..638
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 655 AA; 70001 MW; F81220146804BC6F CRC64;
MARSTIVLRG LRREYPSGEA TVVALRDLDL TIEPGEMVAV MGASGSGKST LMNILGCLDR
PSSGSYQIAG RETASLDADE LAALRREHFG FIFQRYHLLP ELSALSNVEI PAIYAGQSRD
ERRDRANGLL ARLGITDRAS HRPNQLSGGQ QQRVSIARAL MNGADVILAD EPTGALDRRS
GDEVLRILDE LHADGKTVII VTHDASVAAR AKRVIELSDG VVIADRATST VSPAVAAPTA
AAAQAQPRSR WPWQSRLDRI GEAFRMAMLA MAAHRLRTFL TMLGIIIGIA SVVFIVAVGD
AAKRKVLADI SSLGTNTIEI FPGKDLGDVR SSKIKTLVVA DARALRLQPY IDGVTPTVST
SSTLRHGPLE ANALVNGVGD QYFAVKGTKL SAGRFFDADG LRDVSQDVVI DEKTRQTFFS
DDPDGPIGKV LLVGRVPCRI IGVTQQQQGG FGSSQNLSVY LPYTTVQARF LGNSSLRSIL
VKVNDEVTTK AAELDVTRFL TLRHRVKDFV ILNTDDIRKT ITNTTETLTL MIAAIAVISL
VVGGIGVMNI MLVSVSERVG EIGVRMAVGA RRSDILQQFL IEAVMVCLIG GGLGVAVAYG
LAATFNALVP MFQLGLSAGS IIAAFICSTG IGVVFGYLPA RQASFLDPLA ALSRD