MACB2_YERPN
ID MACB2_YERPN Reviewed; 649 AA.
AC Q1CGD7; C4GVW3;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=YPN_2615;
GN ORFNames=YP516_2949;
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; ABG18943.1; -; Genomic_DNA.
DR EMBL; ACNQ01000017; EEO75063.1; -; Genomic_DNA.
DR RefSeq; WP_002211351.1; NZ_ACNQ01000017.1.
DR AlphaFoldDB; Q1CGD7; -.
DR SMR; Q1CGD7; -.
DR EnsemblBacteria; ABG18943; ABG18943; YPN_2615.
DR GeneID; 66842174; -.
DR KEGG; ypn:YPN_2615; -.
DR HOGENOM; CLU_000604_78_3_6; -.
DR OMA; VVILITH; -.
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..649
FT /note="Macrolide export ATP-binding/permease protein MacB
FT 2"
FT /id="PRO_0000269991"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 524..544
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 608..628
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT DOMAIN 5..243
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT BINDING 41..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ SEQUENCE 649 AA; 70346 MW; 53762DD8C3924496 CRC64;
MAALLELEGI RRSYQSGEEI VDVLQDVSLT INAGELVAII GASGSGKSTL MNILGCLDKP
SAGIYRVAGQ NVDELDDDAL AALRREHFGF IFQRYHLLPH LSAAHNVEVP AVYAGLGKHE
RRERANMLLT RLGLGDRVSY QPNQLSGGQQ QRVSIARALM NGGQVILADE PTGALDSHSS
VEVMAILKQL QQQGHTVIIV THDPTVAAQA ERVIEIKDGR IMADSGSKNE PVVAAAELMS
LTPAAPSWQQ LVGRFREALL MAWRAMSANK MRTALTMLGI IIGIASVVSI LVVGDAAKQL
VLADIRAIGT NTIDIYPGKD FGDDDPSTRQ ALVHDDMAAL KAQSYVSAVS PSIGGSMRLR
FGNIDVAASV LGVSDEYFRV FGMAMEQGAP ITREQVERQA QTVVIDLNTQ RRLFPHMKDV
VGQVILVGNM PATVVGVVAE KKSMFGSNKA LRVWVPYSTM ANRLMGRSYF DSITIRIKEG
YSSKEAEQQL VRLLTLRHGK KDIFTYNMDS LLQTAEKTTQ TMQLFLTLVA VISLVVGGIG
VMNIMLVSVT ERTREIGIRM AVGARSSDVM QQFLIEAVLV CLIGGALGIS LSFAIGLIVE
MFLPNWRIAF PPMALFSAFL CSTVIGVVFG YLPARSAARL NPIDALARE
