MACB_RHOP2
ID MACB_RHOP2 Reviewed; 654 AA.
AC Q2IXX0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=RPB_2235;
OS Rhodopseudomonas palustris (strain HaA2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HaA2;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL Submitted (JAN-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; CP000250; ABD06940.1; -; Genomic_DNA.
DR RefSeq; WP_011441127.1; NC_007778.1.
DR AlphaFoldDB; Q2IXX0; -.
DR SMR; Q2IXX0; -.
DR STRING; 316058.RPB_2235; -.
DR EnsemblBacteria; ABD06940; ABD06940; RPB_2235.
DR KEGG; rpb:RPB_2235; -.
DR eggNOG; COG0577; Bacteria.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_78_1_5; -.
DR OMA; NEIGVRM; -.
DR OrthoDB; 1181903at2; -.
DR Proteomes; UP000008809; 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; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..654
FT /note="Macrolide export ATP-binding/permease protein MacB"
FT /id="PRO_0000269972"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 584..604
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 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 654 AA; 69583 MW; FC8894D2D6367C6E CRC64;
MAGSTIELRG LRREFPSGEA TVVALQDLDL TIEPGEMVAI MGASGSGKST LMNILGCLDR
PTSGSYRIAG RETSSLEADE LSALRREHFG FIFQRYHLLP ALSALGNVEI PAIYAGQPGE
ARRARAGELL ARLGLADRSG HRPNQLSGGQ QQRVSIARAL MNGADVILAD EPTGALDQRS
GTEVLQILDE LNRDGKTVII VTHDASVAAR AKRVIELRDG VVVADRLTSP EAARRAGDAP
TRQPPATPRW NWRREYDRIS EATRIAVLAM AAHRLRSFLT MLGIIIGIAS VVFVVAVGDA
AKRKVLADIS SLGTNTIEIF PGKDMGDVRS SKIKTLVAAD ARALAQQPYI DGVTPTVSTT
STLRYGGLEA NALVNGVGDQ YFDVKGTKLA SGRFFDASGL RDIVQDVVID EKTRQTFFAD
VAGGAVGKVI LIGKVPCRIV GVMQQQQSGF GSNQNLSVYL PYTTVQARFL GNSSLRSILL
KVSDTVATAD AEQDVTRFLT LRHRVKDFVI LNTDDIRKTI TSTTGTLTLM IAAIAVISLV
VGGIGVMNIM LVSVSERVGE IGVRMAVGAR RSDILQQFLI EAVVVCLIGG GLGVGVAFGL
AALFNLVVPM FPLSLSGTSI AAAFVCSTGI GIVFGYLPAR QASFLDPLAA LSRD