ID   MACB3_PARDP             Reviewed;         640 AA.
AC   A1BCE9;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Macrolide export ATP-binding/permease protein MacB 3 {ECO:0000255|HAMAP-Rule:MF_01720};
DE            EC=7.6.2.- {ECO:0000255|HAMAP-Rule:MF_01720};
GN   Name=macB3 {ECO:0000255|HAMAP-Rule:MF_01720}; OrderedLocusNames=Pden_5133;
OS   Paracoccus denitrificans (strain Pd 1222).
OG   Plasmid pPD1222.
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 plasmid 1 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; CP000491; ABL73193.1; -; Genomic_DNA.
DR   RefSeq; WP_011751351.1; NC_008688.1.
DR   AlphaFoldDB; A1BCE9; -.
DR   SMR; A1BCE9; -.
DR   STRING; 318586.Pden_5133; -.
DR   PRIDE; A1BCE9; -.
DR   EnsemblBacteria; ABL73193; ABL73193; Pden_5133.
DR   KEGG; pde:Pden_5133; -.
DR   eggNOG; COG0577; Bacteria.
DR   eggNOG; COG1136; Bacteria.
DR   HOGENOM; CLU_000604_78_2_5; -.
DR   OMA; VVILITH; -.
DR   Proteomes; UP000000361; Plasmid pPD1222.
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; 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; 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; Plasmid; Reference proteome; Translocase;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..640
FT                   /note="Macrolide export ATP-binding/permease protein MacB
FT                   3"
FT                   /id="PRO_0000280170"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        519..539
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        560..580
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        581..601
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        606..626
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   DOMAIN          4..242
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ   SEQUENCE   640 AA;  66533 MW;  D078238E4B22EE5B CRC64;
     MPLIRIRGLH RVFGEGAARA HVLRGIDLDI HAGEFVAIVG TSGSGKSTLM NILGLLDRPS
     AGSYHLAGKD VARLSRDARA GLRNRLFGFV FQQYNLIPTL TALENVELPA SHAGAAREAR
     RARAAALLRS LGLGHRLTAR PLQMSGGQQQ RVSIARALMN GGAVILADEP TGALDAESGR
     QVMRLLSDLA GRGHTVILIT HDTDIAARAG RVIRVGEGRI AGDSGTRAAG PAVPVLPETT
     GSRSAFLHAL REAARSALAA IGASPVRTAL TLSGIVIGVA SVVAMLAIGR GAQEEFVKRA
     SAIGTNWVVV GSDQDTRMPR RPLTLDDAMA LKGLPNVAGV MPGRWEQATV RAGAFSIDTD
     IIGTDRDFRG VHGWDVVRGS FFSEADERGG SPVLLLGSTV AGTLFPDGRD PTGEFVFVNM
     SPFLVGGVLE SKGLSENGSD RDKVVAMPLR SLESRVYGPG ELSVIVVALQ DMARLDESNA
     LLREAMIRRH GTEDFWLADA AGAFAAAEAD RASQNLLLGA VATISIFVGG IGVMNIMFIT
     VRERTREIGI RSATGAAMRD ILVQFLTEAT VLSALGGLAG LALAVGIGAV AALGLGMPVV
     FSVTVALGAL AGATAMGAAF GLVPAIRAAR LSPVEALASP