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MACB2_PSEE4
ID   MACB2_PSEE4             Reviewed;         654 AA.
AC   Q1I7I9;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Macrolide export ATP-binding/permease protein MacB 2 {ECO:0000255|HAMAP-Rule:MF_01720};
DE            EC=7.6.2.- {ECO:0000255|HAMAP-Rule:MF_01720};
GN   Name=macB2 {ECO:0000255|HAMAP-Rule:MF_01720}; OrderedLocusNames=PSEEN3665;
OS   Pseudomonas entomophila (strain L48).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=384676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L48;
RX   PubMed=16699499; DOI=10.1038/nbt1212;
RA   Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA   Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA   Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT   "Complete genome sequence of the entomopathogenic and metabolically
RT   versatile soil bacterium Pseudomonas entomophila.";
RL   Nat. Biotechnol. 24:673-679(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; CT573326; CAK16390.1; -; Genomic_DNA.
DR   RefSeq; WP_011534771.1; NC_008027.1.
DR   AlphaFoldDB; Q1I7I9; -.
DR   SMR; Q1I7I9; -.
DR   STRING; 384676.PSEEN3665; -.
DR   PRIDE; Q1I7I9; -.
DR   EnsemblBacteria; CAK16390; CAK16390; PSEEN3665.
DR   KEGG; pen:PSEEN3665; -.
DR   eggNOG; COG0577; Bacteria.
DR   eggNOG; COG1136; Bacteria.
DR   HOGENOM; CLU_000604_78_2_6; -.
DR   OMA; VVILITH; -.
DR   OrthoDB; 1181903at2; -.
DR   Proteomes; UP000000658; 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..654
FT                   /note="Macrolide export ATP-binding/permease protein MacB
FT                   2"
FT                   /id="PRO_0000280173"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        529..549
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        596..616
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        617..637
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   654 AA;  69628 MW;  EF96C8CB11B25740 CRC64;
     MSAPLIELCD IRKAYGGIDS PKVEVLRGIS LSIHPGEFVA IVGASGSGKS TLMNILGCLD
     RPTSGSYRFA GRDVAELDSD ELAWLRREAF GFVFQGYHLI PSGSAQENVE MPAIYAGTPP
     AERHARALAL LDRLGLASRT GNRPHQLSGG QQQRVSIARA LMNGGHIILA DEPTGALDSH
     SGAEVMALLD ELASQGHVII LITHDREVAA RAQRIIEIRD GQMVSDSAAS QPSPAQPEQL
     QANDLRQRLD RGAILKGAWK GEMIEALQAA WRVMWINRFR TALTLLGIII GVASVVVMLA
     VGEGSKRQVM AQMAAFGSNI LYLNGKRATA QEPGGIVTLD DVAAIGELPQ VLHVMPVIGG
     QLMVRQGNSS QKFYVGGNNT WFPAIFNWPV VEGTFFSEAD EASGAAVAVI GQKVRSKMFG
     EGSNPLGQYL LIGNVPFQVV GILAAKGASS GSEDSDERIV VPYSAASIRL FGSHDPEYVA
     IAAIDSRRVN ETEAAIDRLL RQRHQGKHDF DLTNDAALIQ AEARTQNSLS LMLGAIAAIS
     LLVGGIGVMN IMLMTVRERT REIGIRMATG ARQRDILRQF LTEAVMLSMV GGVTGIVIAL
     LVGGGLLLAD IAVAFALPAI LGAFACAVIT GVVFGFMPAR KAARLDPVKA LTSE
 
 
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