MACB1_PARDP
ID MACB1_PARDP Reviewed; 668 AA.
AC A1B677;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Macrolide export ATP-binding/permease protein MacB 1/2 {ECO:0000255|HAMAP-Rule:MF_01720};
DE EC=7.6.2.- {ECO:0000255|HAMAP-Rule:MF_01720};
GN Name=macB1 {ECO:0000255|HAMAP-Rule:MF_01720}; OrderedLocusNames=Pden_2937;
GN and
GN Name=macB2 {ECO:0000255|HAMAP-Rule:MF_01720}; OrderedLocusNames=Pden_3444;
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=318586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222;
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 Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 2 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-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; CP000490; ABL71021.1; -; Genomic_DNA.
DR EMBL; CP000490; ABL71515.1; -; Genomic_DNA.
DR RefSeq; WP_011749211.1; NC_008687.1.
DR AlphaFoldDB; A1B677; -.
DR SMR; A1B677; -.
DR STRING; 318586.Pden_2937; -.
DR PRIDE; A1B677; -.
DR EnsemblBacteria; ABL71021; ABL71021; Pden_2937.
DR EnsemblBacteria; ABL71515; ABL71515; Pden_3444.
DR KEGG; pde:Pden_2937; -.
DR KEGG; pde:Pden_3444; -.
DR eggNOG; COG0577; Bacteria.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_78_1_5; -.
DR OMA; NEIGVRM; -.
DR Proteomes; UP000000361; Chromosome 2.
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..668
FT /note="Macrolide export ATP-binding/permease protein MacB
FT 1/2"
FT /id="PRO_0000280169"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 541..561
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 598..618
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 634..654
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT DOMAIN 9..247
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT REGION 230..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..255
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ SEQUENCE 668 AA; 69941 MW; D5BDAFF6AE0705B6 CRC64;
MAETGAPLIR LRGVGREYPS GEGVLRVLTD IDLDIGQGEF VAVMGASGSG KSTLMNILGC
LDRPSSGSYR MDGREVARLG AGELAALRRE TFGFIFQRYH LLSEMTALGN VEVPAIYRGL
PADARRARAR DLLERLGLGD RTGHRPGQLS GGQQQRVSIA RALVNDARVI LADEPTGALD
SRSGDEVLGI LERLNAEGRT VVIVTHDPRV AARAHRVVEI ADGRIVADRR TGAPAADPGP
GPAQAPQPAP QPAPVQAPVQ ARVQARAAVP VLGRLAEALR MALLSMRAHK LRSFLTMLGI
IIGIASVVSV VALGEGSRRQ VLQNIAGLGT NTLQIFPGRD FGDMRSGRVT TLVTADAAAL
ARQPHVASVS PTVGTSATLR HGATEASAQI SGVGEQYFDV AGVALTQGRG FDEADVAAMG
QNVVIDENTR TSLFGDGPAL GQVFMAGKVP LRVIGVAEAQ NRGPGGSTSL TVYAPYTTVQ
ARYLGSTSVS GLTLRVADDV DMALAEQMVA DILTRRHGTR DFFIVNNDQI RQTITSTTQT
LALLIAAIAV ISLVVGGIGV MNIMLVSVTE RIGEIGLRMA VGARRGDIRA QFLIEAVLVC
VIGGIAGILA ALGFGLAFER MSSDFTLVYS PLSMLAALAS ACAIGLAFGY LPAVNAAKLD
PVKALQKG
