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MACB1_PSEF5
ID   MACB1_PSEF5             Reviewed;         652 AA.
AC   Q4KES7;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 113.
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=PFL_2149;
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(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}.
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DR   EMBL; CP000076; AAY91423.1; -; Genomic_DNA.
DR   RefSeq; WP_011060450.1; NC_004129.6.
DR   AlphaFoldDB; Q4KES7; -.
DR   SMR; Q4KES7; -.
DR   STRING; 220664.PFL_2149; -.
DR   PRIDE; Q4KES7; -.
DR   EnsemblBacteria; AAY91423; AAY91423; PFL_2149.
DR   GeneID; 57475185; -.
DR   KEGG; pfl:PFL_2149; -.
DR   PATRIC; fig|220664.5.peg.2178; -.
DR   eggNOG; COG0577; Bacteria.
DR   eggNOG; COG1136; Bacteria.
DR   HOGENOM; CLU_000604_78_1_6; -.
DR   OMA; NEIGVRM; -.
DR   OrthoDB; 1181903at2; -.
DR   Proteomes; UP000008540; 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; Reference proteome; Translocase;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..652
FT                   /note="Macrolide export ATP-binding/permease protein MacB
FT                   1"
FT                   /id="PRO_0000269957"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        525..545
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        586..606
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        615..635
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   DOMAIN          6..244
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   BINDING         42..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ   SEQUENCE   652 AA;  70768 MW;  C938D71B46FE73D5 CRC64;
     MSEPLLHLTG ISRSFTAGDR EFLALKHIDL SIQAGEMVAI TGASGSGKST LMNILGCLDY
     ATAGSYKVNG RETRDLDDQA LAELRRDYFG FIFQRYHLLP HLSAMHNVEM PAIYAGTPQV
     RRHGRARELL ARLGLSGHLG HRPSQLSGGQ QQRVSIARAL MNGGEVILAD EPTGALDTAS
     GKEVMNILQE LHGLGHTVII VTHDPKVAAN AQRIIEVRDG EIVSDRANPR PADEAPSEPP
     VSVRPAGARR LVASLGLFKE AFVMAWVALV SHRMRTLLTM LGIVIGITSV VSIVAIGEGA
     KRYVLKDIQA IGSNTIDIFP GASFGDSRAA AIQTLMPADV TALNQLYYVD SATPMVGRSL
     LLRYGNIDLN ATVNGVSHLY FQVRDIKLAS GISFSENDAR RQAQVVVIDH NTRNRLFGPD
     VDPLGQVILV GNLPCTVIGV TRENKNMFAA SNLLNVWLPY ETAAGRVLGQ RHLDSISVRI
     KDGQPSKVVE EHVKKLMEQR HGTKDFFTNN LDSIMQTVQR TSRSLALLLS LIAVISLVVG
     GIGVMNIMLV SVTERTREIG IRMAVGARQS DIRQQFLVEA VMVCLIGGAI GISLSFAIGY
     LFTLFIKEWE MVFSMGSIIT AFACSTLIGI VFGFVPARNA ARLDPIEALA RD
 
 
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