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MACB1_AERHH
ID   MACB1_AERHH             Reviewed;         648 AA.
AC   A0KGB3;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Macrolide export ATP-binding/permease protein MacB 1 {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=AHA_0761;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS   13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC
RC   2358 / NCIMB 9240 / NCTC 8049;
RX   PubMed=16980456; DOI=10.1128/jb.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(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; CP000462; ABK38211.1; -; Genomic_DNA.
DR   RefSeq; WP_011704712.1; NC_008570.1.
DR   RefSeq; YP_855302.1; NC_008570.1.
DR   AlphaFoldDB; A0KGB3; -.
DR   SMR; A0KGB3; -.
DR   STRING; 380703.AHA_0761; -.
DR   EnsemblBacteria; ABK38211; ABK38211; AHA_0761.
DR   KEGG; aha:AHA_0761; -.
DR   PATRIC; fig|380703.7.peg.759; -.
DR   eggNOG; COG0577; Bacteria.
DR   eggNOG; COG1136; Bacteria.
DR   HOGENOM; CLU_000604_78_2_6; -.
DR   OMA; NEIGVRM; -.
DR   Proteomes; UP000000756; 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..648
FT                   /note="Macrolide export ATP-binding/permease protein MacB
FT                   1"
FT                   /id="PRO_0000280160"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        521..541
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        578..598
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        613..633
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   REGION          222..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         42..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ   SEQUENCE   648 AA;  69008 MW;  BA2568F2D593661B CRC64;
     MREPLLQLSG IRRHFGDGER RVEVLKGIDL TIARGEMVAI VGASGSGKST LLNILGCLDQ
     PSEGSYRVAG RETSRLTADA LATLRREHFG FIFQRYHLLG DLSARDNVAL PALYAGLAGD
     ARKARAERLL QRLGLGSRLD YKPSQLSGGQ QQRVSIARAL INGGQVILAD EPTGALDSQS
     GAEVLGILGA LHRQGHTLVL VTHDMAIAEQ AERIIELKDG AVVADRRREP TPPSPAPTTS
     RADTGGRGGL AGRLGAAFKM ALLAMRAQRM RTFLTMLGII IGIAAVVSVV ALGRGSQQQV
     LANINAMGTS TLEIFPGSGF GDRRAEAVQT LRVEDAEALA GLGYVHSVTP SLATSVTLRR
     GSQAVLGSVN GVGEQFFQVR GYRLLQGMLF DAASVTALAQ EVVIDENSLA RLFGAGESPL
     GQVILLGSLP CRVIGVVARN QSGFGSDENL NVWIPHTTAM TRMLGQSHLR SISVRVQDEV
     ALAAAEDGIS RLLRERHGAQ DFFVLNTDSI RQAITSTNAT LTLLIAMIAL ISLVVGGIGV
     MNIMLVSVSE RTREIGVRMA VGARTGDILQ QFLIEAVLVC LLGGAAGVLL SLLIGVLFEH
     FSSQFTLSYS LDAVLMAFFC SSLIGVLFGF FPARRAARMD PIHALERE
 
 
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