MACB1_YERPN
ID MACB1_YERPN Reviewed; 678 AA.
AC Q1CJW8; C4GRZ6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=YPN_1382;
GN ORFNames=YP516_1524;
OS Yersinia pestis bv. Antiqua (strain Nepal516).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=377628;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nepal516;
RA Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000305; ABG17712.1; -; Genomic_DNA.
DR EMBL; ACNQ01000008; EEO77837.1; -; Genomic_DNA.
DR RefSeq; WP_002208496.1; NZ_ACNQ01000008.1.
DR AlphaFoldDB; Q1CJW8; -.
DR SMR; Q1CJW8; -.
DR PRIDE; Q1CJW8; -.
DR EnsemblBacteria; ABG17712; ABG17712; YPN_1382.
DR GeneID; 57975698; -.
DR KEGG; ypn:YPN_1382; -.
DR HOGENOM; CLU_000604_78_1_6; -.
DR OMA; NEIGVRM; -.
DR Proteomes; UP000008936; 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 1"
FT /id="PRO_0000269990"
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; 73871 MW; CA7A4E3566008299 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 DAVIDENTRD KLFPNGETPL GKVILLGSLP CRVIGVAAKK QSGFGSDENL
NVWIPYTTAM KRMLGQSYLK SITVRVNDDI DLANAEQGVI KLLSQRHGTQ DFFVMNTDSI
RQTIQATTST MTLLVSMIAV ISLIVGGIGV MNIMLVSVTE RTKEIGVRMA VGARASDIMQ
QFLIEAVLVC LLGGSLGVAL SLGIGLLFSL FSSNFSMVYS AASIITAFVC SSLIGVIFGF
FPAKRAAEMD PIRALERE
