MACB1_PSESM
ID MACB1_PSESM Reviewed; 656 AA.
AC Q884D4;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=PSPTO_2159;
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}.
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; AE016853; AAO55676.1; -; Genomic_DNA.
DR RefSeq; NP_791981.1; NC_004578.1.
DR RefSeq; WP_005769685.1; NC_004578.1.
DR AlphaFoldDB; Q884D4; -.
DR SMR; Q884D4; -.
DR STRING; 223283.PSPTO_2159; -.
DR EnsemblBacteria; AAO55676; AAO55676; PSPTO_2159.
DR GeneID; 1183806; -.
DR KEGG; pst:PSPTO_2159; -.
DR PATRIC; fig|223283.9.peg.2190; -.
DR eggNOG; COG0577; Bacteria.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_78_2_6; -.
DR OMA; VVILITH; -.
DR OrthoDB; 1181903at2; -.
DR PhylomeDB; Q884D4; -.
DR Proteomes; UP000002515; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:JCVI.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; ISS:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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..656
FT /note="Macrolide export ATP-binding/permease protein MacB
FT 1"
FT /id="PRO_0000269965"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 538..558
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 589..609
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 619..639
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT DOMAIN 6..245
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT BINDING 43..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ SEQUENCE 656 AA; 69582 MW; F552FC0AB1022229 CRC64;
MHTPLIDLRG IRKSYGGGDS PRVNVLRGID LSIHAGEFVA IVGASGSGKS TLMNILGCLD
RPTSGEYLFA GENVAELGGD ELAWLRREAF GFVFQGYHLI PSGSAQENVE MPAIYAGTPA
AERHARAAAL LDRLGLASRT GNRPHQLSGG QQQRVSIARA LMNGGHIILA DEPTGALDSH
SGAEVMTLLD ELASQGHVVI LITHDREVAA RANRVIEISD GLVISDTARD LSTPRSANPA
ALQAVDLRKR LSEGSGSHGA WKGELLDAIQ AAWRVMWVNR FRTALTLLGI VIGVASVVVM
LAVGEGSKRQ VMAQMSSFGS NIIYLNGKAP NPRAPKGVIT LEEVAALGEL PEVKMIMPVN
GGQAGVRFGN VDHSSYVGGN DTHFPAIFNW PVAEGSYFSE ADEQGAAAVA VIGYKVRQKL
FGDRIDPIGQ YILIENVPFQ VVGVLQEKGA TSGDLDSDNR IAIPYSSASI RLFGSQDPEY
ITIATRDANN VKQAEAAIRT LLQRLHNGKQ DYELTNNAAM IQAEARTQNT LSLMLGSIAA
ISLLVGGIGV MNIMLMTVRE RTREIGIRMA TGARQRDILR QFLTEAVMLS VVGGLAGIVL
ALAMGAALLA SKVAVAFTLS AVIGAFACAL VTGVIFGFMP ARKAARLDPV AALTSE
