ID   MACB2_YERPS             Reviewed;         678 AA.
AC   Q668L6;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Macrolide export ATP-binding/permease protein MacB 2 {ECO:0000255|HAMAP-Rule:MF_01720};
DE            EC=7.6.2.- {ECO:0000255|HAMAP-Rule:MF_01720};
GN   Name=macB2 {ECO:0000255|HAMAP-Rule:MF_01720}; OrderedLocusNames=YPTB2721;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(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; BX936398; CAH21959.1; -; Genomic_DNA.
DR   RefSeq; WP_011192738.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q668L6; -.
DR   SMR; Q668L6; -.
DR   EnsemblBacteria; CAH21959; CAH21959; YPTB2721.
DR   GeneID; 66844852; -.
DR   KEGG; yps:YPTB2721; -.
DR   OMA; NEIGVRM; -.
DR   Proteomes; UP000001011; 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; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..678
FT                   /note="Macrolide export ATP-binding/permease protein MacB
FT                   2"
FT                   /id="PRO_0000269993"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        558..578
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        608..628
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        641..661
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   DOMAIN          11..249
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   BINDING         47..54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ   SEQUENCE   678 AA;  73885 MW;  8F7A4E35D6008299 CRC64;
     MTGPQQGKIL LRLENVSREF ITGEQTVRVL NNINLTLHSG EMVAIVGTSG SGKSTLMNIL
     GCLDKPSAGE YWVAGRIPQY LGSDALAELR REHFGFIFQR YHLLNDLSAR ENVEIPAIYA
     GIDREERRKR AVNLLSRIGL AERLDYRPSQ LSGGQQQRVS IARALMNGGD VILADEPTGA
     LDTHSGNEVL NILKDLHQQG HTVVIVTHDM SIAEHAQRII ELKDGEIIAD RPRDHAQEKP
     KMVDIPSVID IPSMDEKIST GAQQETEIAR KPLLTRWKVQ YDRLHEAFKM AILAMAAQRL
     RTALTMLGII IGIASVVSVV ALGKGSQQQV LANINAMGTS TLEIFPGKDF GDMRSAAIHT
     LRDTDADVLA QQGYIHSVTP TVSTSVTLRY GNKSVSGTVN GVGEQYFLVR GYTIAQGMAF
     TRTSVNDLMQ EAVIDENTRD KLFPNGETPL GKVILLGSLP CRVIGVAAKK QSGFGSDENL
     NVWIPYTTAM KRMLGQSYLK SITVRVNDDI DLANAEQGVI KLLSQRHGTQ DFFVMNTDSI
     RQTIQATTST MTLLVSMIAV ISLIVGGIGV MNIMLVSVTE RTKEIGVRMA VGARASDIMQ
     QFLIEAVLVC LLGGSLGVAL SLGIGLLFSL FSSNFSMVYS AASIITAFVC SSLIGVIFGF
     FPAKRAAEMD PIRALERE