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MACB_PECAS
ID   MACB_PECAS              Reviewed;         650 AA.
AC   Q6D8T5;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=ECA0887;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; BX950851; CAG73799.1; -; Genomic_DNA.
DR   RefSeq; WP_011092490.1; NC_004547.2.
DR   AlphaFoldDB; Q6D8T5; -.
DR   SMR; Q6D8T5; -.
DR   STRING; 218491.ECA0887; -.
DR   EnsemblBacteria; CAG73799; CAG73799; ECA0887.
DR   KEGG; eca:ECA0887; -.
DR   PATRIC; fig|218491.5.peg.890; -.
DR   eggNOG; COG0577; Bacteria.
DR   eggNOG; COG1136; Bacteria.
DR   HOGENOM; CLU_000604_78_1_6; -.
DR   OMA; NEIGVRM; -.
DR   OrthoDB; 1181903at2; -.
DR   Proteomes; UP000007966; 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..650
FT                   /note="Macrolide export ATP-binding/permease protein MacB"
FT                   /id="PRO_0000269938"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        523..543
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        580..600
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        615..635
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          227..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..246
FT                   /note="Polar residues"
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   650 AA;  70465 MW;  BB2E671380578755 CRC64;
     MSTSLLKLTG ITRRFTNGEQ DVTVLKDINL TINQGEMVAI VGASGSGKST LMNILGCLDK
     PSAGDYQVAG RAVGKLDNDQ LAELRREHFG FIFQRYHLLG DLTALGNVEV PAIYAGKSRL
     ARRQRAADLL TRLGLENRLH YRPSQLSGGQ QQRVSIARAL MNAGGIILAD EPTGALDTHS
     GNEVLSILRD LHRQGNTVVI VTHDMTIAEH AQRVIELRDG EVIADRQTRP EEATASSPEA
     ASSPATSALN QFKDRFIDAF KMALLAMNAQ RMRTFLTMLG IIIGIASVVS VVALGKGSQE
     QVLANINSMG TSTLEIFPGK GFGDMDASAI QTLRASDIQP LTQQPYVHSV TPSVSTSVTM
     RYGNIAVSAS ISGVGEQFFT VRGYTLERGV LFPRSSVDEL TQDAVIDKNT RDKLFPHGED
     PIGQVILVGS LPVRIIGVVS KNQGGFGSDE NLNVWVPYTT VMKRMVGQSY LKSITVRVKD
     NVDMSIAEQR ITDLLMQRHG TKDFFIMNTD SIRQMIEKTT TTLTLLVSMI ALISLLVGGI
     GVMNIMLVSV TERTREIGVR MAVGARTSDI MQQFLIEAVL VCLFGGIAGV ALSLAIGVLF
     AQLSSNFAMI YSSSSIIAAF LCSSLIGIIF GFFPARRAAR MEPIHALERE
 
 
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