MACB_WOLSU
ID MACB_WOLSU Reviewed; 643 AA.
AC Q7M8U0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=WS1418;
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC 11488 / FDC 602W;
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
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; BX571660; CAE10481.1; -; Genomic_DNA.
DR RefSeq; WP_011139266.1; NC_005090.1.
DR AlphaFoldDB; Q7M8U0; -.
DR SMR; Q7M8U0; -.
DR STRING; 273121.WS1418; -.
DR EnsemblBacteria; CAE10481; CAE10481; WS1418.
DR KEGG; wsu:WS1418; -.
DR eggNOG; COG0577; Bacteria.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_78_2_7; -.
DR OMA; VVILITH; -.
DR OrthoDB; 1181903at2; -.
DR Proteomes; UP000000422; 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; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..643
FT /note="Macrolide export ATP-binding/permease protein MacB"
FT /id="PRO_0000269985"
FT TRANSMEM 270..290
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 569..589
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 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 643 AA; 70008 MW; 7D5F705827B9DA35 CRC64;
MQKPLIELKG VSRVFNLGGL AVEVLKGIDL QIYPGEFVAI MGASGSGKST LMNILGCLDR
PSQGEYLFRG ESVSLLHRDD LAQLRREEFG FIFQSYHLIH ALDARENVEV PAIYAGAGIV
EREKRAEELL GSLGLGERLH HRPSQLSGGQ QQRVSIARAL MNGGRVILAD EPTGALDSRS
GEEVMQLLME LSRQGHTIIL ITHDSHVASH ANRVIEMKDG QITHRQEPVI RESNQVRSPF
GVRHSSILLE LFEAMKMAFR SLKMNLFRTV LTLLGIVIGV ASVIVMLAIG DGAKNAVLER
ISAMGTNILV IRPGMPNSRG FSNIATLIPE DMEAIMELDN IIAAMPENKK SVTTRYGNND
QSTSLNATSS HFTKVRNWPL GKGVFFTEED EKSYAKVVVL GKTVEKALFG EEDALGRFIL
VDNIMFQIIG VMSNRGASAS GEDEDDVILV PYTTGSLHLI GQKFLRNITV AVDDLSRMGE
TEREIHSLLL ARHGGIEDFR IRNMASLIED VTQTQNTLTI LLGSIAAISL LVGGIGVMNI
MLVSVTERTK EIGIRIATGA RMRHILQQFL IEAVVVSALG GLIGVVIGLG VSALIEGLGT
PVYYSLMPIV WAFGCAFVTG LLFGYLPARK AARLDPVVAL ASE