MACB_PSEAE
ID MACB_PSEAE Reviewed; 663 AA.
AC Q9I190; Q5DIQ4; Q5DIS1; Q5DIV0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
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=PA2390;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MSH, R', and Serotype 13;
RX PubMed=15743962; DOI=10.1128/jb.187.6.2138-2147.2005;
RA Smith E.E., Sims E.H., Spencer D.H., Kaul R., Olson M.V.;
RT "Evidence for diversifying selection at the pyoverdine locus of Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 187:2138-2147(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AY765260; AAX16304.1; -; Genomic_DNA.
DR EMBL; AY765262; AAX16333.1; -; Genomic_DNA.
DR EMBL; AY765263; AAX16350.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG05778.1; -; Genomic_DNA.
DR PIR; H83346; H83346.
DR RefSeq; NP_251080.1; NC_002516.2.
DR RefSeq; WP_003114506.1; NZ_QZGE01000021.1.
DR AlphaFoldDB; Q9I190; -.
DR SMR; Q9I190; -.
DR STRING; 287.DR97_6042; -.
DR PaxDb; Q9I190; -.
DR PRIDE; Q9I190; -.
DR EnsemblBacteria; AAG05778; AAG05778; PA2390.
DR GeneID; 882237; -.
DR KEGG; pae:PA2390; -.
DR PATRIC; fig|208964.12.peg.2501; -.
DR PseudoCAP; PA2390; -.
DR HOGENOM; CLU_000604_78_2_6; -.
DR InParanoid; Q9I190; -.
DR OMA; VVILITH; -.
DR PhylomeDB; Q9I190; -.
DR BioCyc; PAER208964:G1FZ6-2428-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:1990281; C:efflux pump complex; IDA:PseudoCAP.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IDA:PseudoCAP.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0002049; P:pyoverdine biosynthetic process; IMP:PseudoCAP.
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; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..663
FT /note="Macrolide export ATP-binding/permease protein MacB"
FT /id="PRO_0000269956"
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"
FT CONFLICT 6
FT /note="Q -> H (in Ref. 1; AAX16304)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="I -> T (in Ref. 1; AAX16333/AAX16350)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="E -> A (in Ref. 1; AAX16333)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="H -> Q (in Ref. 1; AAX16304)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 663 AA; 70861 MW; 9D588D4EF4FA10DB CRC64;
MENATQPVPL IELRDIRKRY GGNGTPEVEV LKGVSLSIHA GEFVAIVGAS GSGKSTLMNI
LGCLDRPSSG SYHFAGHDVA ELDSDEQAWL RREAFGFVFQ GYHLIPSASA QENVEMPAIY
AGIPASERHT RARALLERLG LAERTANRPH QLSGGQQQRV SIARALMNGG HIILADEPTG
ALDSHSGAEV MALLDELASQ GHVVILITHD RDVAARAKRI IEVRDGEIVS DSANDERPAH
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
