MACB_PSEAB
ID MACB_PSEAB Reviewed; 663 AA.
AC Q02MI4;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Macrolide export ATP-binding/permease protein MacB {ECO:0000255|HAMAP-Rule:MF_01720};
DE EC=7.6.2.- {ECO:0000255|HAMAP-Rule:MF_01720};
GN Name=macB {ECO:0000255|HAMAP-Rule:MF_01720}; OrderedLocusNames=PA14_33760;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ11567.1; -; Genomic_DNA.
DR RefSeq; WP_003139295.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02MI4; -.
DR SMR; Q02MI4; -.
DR PRIDE; Q02MI4; -.
DR EnsemblBacteria; ABJ11567; ABJ11567; PA14_33760.
DR KEGG; pau:PA14_33760; -.
DR HOGENOM; CLU_000604_78_2_6; -.
DR OMA; VVILITH; -.
DR BioCyc; PAER208963:G1G74-2840-MON; -.
DR Proteomes; UP000000653; 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..663
FT /note="Macrolide export ATP-binding/permease protein MacB"
FT /id="PRO_0000280171"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 598..618
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 626..646
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT DOMAIN 11..250
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT BINDING 48..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ SEQUENCE 663 AA; 70861 MW; 7889064B87D64581 CRC64;
MENATHPVPL IELRDIRKRY GGNGTPEVEV LKGVSLSIHA GEFVAIVGAS GSGKSTLMNI
LGCLDRPSSG SYHFAGHDVA ELDSDEQAWL RREAFGFVFQ GYHLIPSASA QENVEMPAIY
AGIPASERHT RARALLERLG LAERTANRPH QLSGGQQQRV SIARALMNGG HIILADEPTG
ALDSHSGAEV MALLDELASQ GHVVILITHD RDVAARAKRI IEVRDGEIVS DSANDERPAQ
PSAGVERHLQ ADDLSQRLAE GSSEPSGAWR AELLEAVRAA WRVMWINRFR TALTLLGIII
GVASVVVMLA VGEGSKRQVM AQMGAFGSNI IYLSGYSPNP RAPMGIVSSD DVAAIATLPQ
VKKVMPVNGG ELVVRYGNID YHAYVGGNNT DFPEILNWPV AEGSYFTERD EDAATTVAVI
GYKVRKKLFG SANPIGRYIL IENVPFQVIG VLAEKGSSSG DKDADNRIAI PYSAASIRLF
GTRNPEYVII AAADAQRVHQ AERAIDQLML RLHRGQRDYE LTNNAAMIQA EAKTQNTLSL
MLGSIAAISL LVGGIGVMNI MLMTVRERTR EIGIRMATGA RQGDILRQFL TEAAMLSVVG
GLAGIALALC IGGVLLLGQV AVAFSLSAIV GAFSCALVTG LVFGFMPARK AAQLDPVAAL
ASQ