MACB2_PSESM
ID MACB2_PSESM Reviewed; 668 AA.
AC Q881Q1;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=PSPTO_2832;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO56331.1; -; Genomic_DNA.
DR RefSeq; NP_792636.1; NC_004578.1.
DR RefSeq; WP_011104221.1; NC_004578.1.
DR AlphaFoldDB; Q881Q1; -.
DR SMR; Q881Q1; -.
DR STRING; 223283.PSPTO_2832; -.
DR EnsemblBacteria; AAO56331; AAO56331; PSPTO_2832.
DR GeneID; 1184486; -.
DR KEGG; pst:PSPTO_2832; -.
DR PATRIC; fig|223283.9.peg.2891; -.
DR eggNOG; COG0577; Bacteria.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_78_1_6; -.
DR OMA; NEIGVRM; -.
DR OrthoDB; 1181903at2; -.
DR PhylomeDB; Q881Q1; -.
DR Proteomes; UP000002515; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:JCVI.
DR GO; GO:0005524; F:ATP binding; ISS:JCVI.
DR GO; GO:0046677; P:response to antibiotic; ISS:JCVI.
DR GO; GO:0042908; P:xenobiotic transport; ISS:GO_Central.
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..668
FT /note="Macrolide export ATP-binding/permease protein MacB
FT 2"
FT /id="PRO_0000269966"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 541..561
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 602..622
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 631..651
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT DOMAIN 22..260
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT REGION 242..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ SEQUENCE 668 AA; 72496 MW; 973BED16B6A1030B CRC64;
MNQKVDIEAL HETSINSDQP LLRLQQVSRS FMAGDREFQV LKHIDLAIHT GELVAIIGAS
GSGKSTLMNI LGCLDHASAG SYQVNGQETR ELDDDALAAL RRDHFGFIFQ RYHLLPHLDA
VRNVEIPAIY AGTAQTTRHE RAQALLTRLG LGGHLQHRPS QMSGGQQQRV SIARALMNGG
QVILADEPTG ALDTASGKEV MRTLLELHAA GHTVILVTHD PKVAANAERI IEVSDGEIIS
DRRTAQTTQP APEAQPATPP GPAPRRLLAS LGLFREAFNM AWIALISHRM RTLLTMLGII
IGITSVVSIS AIGEGAKRYV LKDIQSIGSN TIDIYAGANF GDSRAKSIET LLPSDVAALN
QLYYIDSATP VVGRSMLVRY RNVDVDAQLN GVSSRYFQVR NIQLAAGITF SDQDARRQAQ
VVVLDHNTAQ RLFGPGVNPL GQVILVGKLP CTVIGVTSDH KNLFIAGNTL NLWMPYETAA
GRVLGQRHLD SISVRVKDGM PSKAVEEQIK ALMLQRHGTK DFFTNNLDSV MQTVQKTSRS
LTLLLSLIAV ISLVVGGIGV MNIMLVSVTE RTREIGIRMA VGARQSDIRQ QFLVEAVMVC
LMGGVIGIGL SYAIGYLFTL FVQQWEMVFS LASVVTAFAC STLIGVLFGF VPARNAARLD
PIEALARD
