MACB1_PSEU2
ID MACB1_PSEU2 Reviewed; 657 AA.
AC Q4ZV10;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=Psyr_1969;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY37012.1; -; Genomic_DNA.
DR RefSeq; WP_011267356.1; NC_007005.1.
DR RefSeq; YP_235050.1; NC_007005.1.
DR AlphaFoldDB; Q4ZV10; -.
DR SMR; Q4ZV10; -.
DR STRING; 205918.Psyr_1969; -.
DR EnsemblBacteria; AAY37012; AAY37012; Psyr_1969.
DR KEGG; psb:Psyr_1969; -.
DR PATRIC; fig|205918.7.peg.2011; -.
DR eggNOG; COG0577; Bacteria.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_78_2_6; -.
DR OMA; VVILITH; -.
DR Proteomes; UP000000426; 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..657
FT /note="Macrolide export ATP-binding/permease protein MacB
FT 1"
FT /id="PRO_0000269963"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 539..559
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 590..610
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 620..640
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 657 AA; 69870 MW; B16D02E3F7745DC0 CRC64;
MRTPLIDLRG IRKSYGGGDS PLVNVLRGID LSIHTGEFVA IVGASGSGKS TLMNILGCLD
RPTSGEYLFA GENVAALGSD ELAWLRREAF GFVFQGYHLI PSGSAQENVE MPAIYAGTPA
AERHARAAAL LDRLGLASRT GNRPHQLSGG QQQRVSIARA LMNGGHIILA DEPTGALDSH
SGAEVMTLLD ELASQGHVVI LITHDREVAA RAKRVIEISD GLVISDTAQD ASDVQRSVNP
AALQAVDLRK RLSEGSGSQS AWQGELFDAI RAAWRVMWIN RFRTALTLLG IVIGVASVVV
MLAVGEGSKR QVMAQMSSFG SNIIYLNGKA PNPRAPKGVI TLEEVAALGE LPEVKMIMPV
NGGQAGVRYG NLDHSSYVGG NDTHFPAIFN WPVVEGSYFS EADEQNAAAV AVIGYKVRQK
LFGEQSDPVG QYILIENVPF QVVGVLQEKG ATSGDLDSDN RIAIPYSSAS IRLFGTQDPE
YITIATRDAN NVKQAEQSIR NLLQQLHHGK QDYELTNNAA MIQAEARTQN TLSLMLGSIA
AISLLVGGIG VMNIMLMTVR ERTREIGIRM ATGARQSDIL RQFLTEAVML SVVGGLAGIV
LALGMGAALL LSKVAVAFTL PAVAGAFACA LITGVIFGFM PARKAARLDP VAALTSE