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MACB_VIBPA
ID   MACB_VIBPA              Reviewed;         654 AA.
AC   Q87JM4;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=VPA0224;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; BA000032; BAC61567.1; -; Genomic_DNA.
DR   RefSeq; NP_799734.1; NC_004605.1.
DR   RefSeq; WP_005481460.1; NC_004605.1.
DR   AlphaFoldDB; Q87JM4; -.
DR   SMR; Q87JM4; -.
DR   STRING; 223926.28808362; -.
DR   EnsemblBacteria; BAC61567; BAC61567; BAC61567.
DR   GeneID; 1190912; -.
DR   KEGG; vpa:VPA0224; -.
DR   PATRIC; fig|223926.6.peg.3179; -.
DR   eggNOG; COG0577; Bacteria.
DR   eggNOG; COG1136; Bacteria.
DR   HOGENOM; CLU_000604_78_1_6; -.
DR   OMA; NEIGVRM; -.
DR   Proteomes; UP000002493; Chromosome 2.
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..654
FT                   /note="Macrolide export ATP-binding/permease protein MacB"
FT                   /id="PRO_0000269984"
FT   TRANSMEM        280..300
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        584..604
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        619..639
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   654 AA;  71213 MW;  FAC428A67A00EF30 CRC64;
     MSDVLLKVED LTRRFVSGDE SLTVLNHINL EIKRGEMVAI VGASGSGKST LMNVLGCLDK
     PSSGRYFING QDVSTLESDQ LAELRREYFG FIFQRYHLLG DLTAVANVEV PAVYAGVPHR
     QRTERAQSLL ARLGLEDRLT HKPSQLSGGQ QQRVSVARAL MNGGEVILAD EPTGALDSHS
     GQEMMALLKE LHQLGHTIIL VTHDMNVANF ADRIIEIKDG EIIADTLNAQ VVINEQAAKT
     PSASFHRPAQ AVSKWWKWDS FIDALKMALL AMSSHRMRTF LTMLGIIIGI ASVVSVVALG
     NGSQQQILSN ISSMGTNTID VRPGKGFGDR RSGRVKTLTA DDAKSLESLP FVDSVTPSLS
     NSLTVRYANQ DATASVEGVG EDYFRVRGYE IAKGQFWDEE SVNSLAQEAV IDDNTRKEMF
     ADRNPIGEVI FLGSLPVRIV GVTQKKEDAF GNSDALKIWV PYTTMSGRMM GQRYLNGITV
     RIDENAPSAA VEQSIINLLK MRHGTEDFFT INTDTIRQSI EKTTATMTLL ISAIAVISLI
     VGGIGVMNIM LVSVTERTKE IGVRMAVGAR QADILRQFLI EAVLVCLCGG IAGIGLAFLI
     GFAFSTSGSS FQMIYSMNSI IWAFICSTLI GIAFGFLPAR NAAKLDPIEA LARD
 
 
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