MACB_ECOLX
ID MACB_ECOLX Reviewed; 646 AA.
AC P0C2H2; Q3L7H3;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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}; Synonyms=etsB;
GN ORFNames=O2ColV34;
OS Escherichia coli.
OG Plasmid pAPEC-O2-ColV.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A2363 / APEC;
RX PubMed=16954398; DOI=10.1128/iai.00363-06;
RA Skyberg J.A., Johnson T.J., Johnson J.R., Clabots C., Logue C.M.,
RA Nolan L.K.;
RT "Acquisition of avian pathogenic Escherichia coli plasmids by a commensal
RT E. coli isolate enhances its abilities to kill chicken embryos, grow in
RT human urine, and colonize the murine kidney.";
RL Infect. Immun. 74:6287-6292(2006).
CC -!- FUNCTION: Part of the tripartite efflux system MacAB-TolC. MacB is a
CC non-canonical ABC transporter that contains transmembrane domains
CC (TMD), which form a pore in the inner membrane, and an ATP-binding
CC domain (NBD), which is responsible for energy generation. Confers
CC resistance against macrolides. {ECO:0000255|HAMAP-Rule:MF_01720}.
CC -!- SUBUNIT: Homodimer. Part of the tripartite efflux system MacAB-TolC,
CC which is composed of an inner membrane transporter, MacB, a periplasmic
CC membrane fusion protein, MacA, and an outer membrane component, TolC.
CC The complex forms a large protein conduit and can translocate molecules
CC across both the inner and outer membranes. Interacts with MacA.
CC {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; AY545598; ABA54762.1; -; Genomic_DNA.
DR RefSeq; WP_000733250.1; NZ_WVVG01000048.1.
DR RefSeq; YP_001711875.1; NC_010409.1.
DR RefSeq; YP_009071137.1; NC_025179.1.
DR RefSeq; YP_444080.1; NC_007675.1.
DR AlphaFoldDB; P0C2H2; -.
DR SMR; P0C2H2; -.
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; Plasmid; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..646
FT /note="Macrolide export ATP-binding/permease protein MacB"
FT /id="PRO_0000269939"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 570..590
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 611..631
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT DOMAIN 5..243
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT BINDING 41..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ SEQUENCE 646 AA; 70385 MW; 01405822AC79BF5F CRC64;
MKKLIELKGV SRTYGNGDQT RTVLKNVDLT IVAGEMVAII GASGSGKSTL MNIMGCLDVP
NRGDYYIDGQ NAACLSPDEL ARVRREHIGF IFQRYHLIPD LSALGNVEIP AIYANSERDS
RRQRATALLG RLGLEGREHH KPCELSGGQQ QRVSIARALI NGGKIILADE PTGALDSQSG
QEVLAILNEL NRRGHTVVMV THDMKVARHA KRIIELCDGE IIADSGGCVS ATETLPKTNR
IRQSYWKTLL DRTRESMQMA LKAMKTHRLR TTLTMIGIVF GIASVVTVVA LGEGARQETL
EEIKSLGTNV VSIYPGQDLF DDSIESIRTL VPADANALAK QGFIDSVSPE VSASDNIRFL
GKSAIASING VGREHFRVKG IELLQGTTFR DDRNALQEVI IDENTRKAIF DNTGLQALGQ
IVFLGSVPAR VVGIAKSNNR SDASNRITVW MPYSTVMYRI VGKPVLTGIS VRLKDNVDNE
AAISAISQLL TRRHGIKDFQ LYNFEQIRKS IEHTSMTFSI LILMVACISL MIGSIGVMNI
MLISVTERTH EIGVRMAVGA RRSDIMQQFI IEAVLVCLIG GALGIALSYI TGALFNALAD
GIFAAIYSWQ AAVAAFFCST LIGIIFGYLP ARKAARMDPV ISLASE
