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MACB_MANSM
ID   MACB_MANSM              Reviewed;         643 AA.
AC   Q65TH4;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=MS1129;
OS   Mannheimia succiniciproducens (strain MBEL55E).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Basfia.
OX   NCBI_TaxID=221988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBEL55E;
RX   PubMed=15378067; DOI=10.1038/nbt1010;
RA   Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA   Jeong H., Hur C.G., Kim J.J.;
RT   "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT   succiniciproducens.";
RL   Nat. Biotechnol. 22:1275-1281(2004).
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; AE016827; AAU37736.1; -; Genomic_DNA.
DR   RefSeq; WP_011200304.1; NC_006300.1.
DR   AlphaFoldDB; Q65TH4; -.
DR   SMR; Q65TH4; -.
DR   STRING; 221988.MS1129; -.
DR   EnsemblBacteria; AAU37736; AAU37736; MS1129.
DR   KEGG; msu:MS1129; -.
DR   eggNOG; COG0577; Bacteria.
DR   eggNOG; COG1136; Bacteria.
DR   HOGENOM; CLU_000604_78_2_6; -.
DR   OMA; NEIGVRM; -.
DR   OrthoDB; 1181903at2; -.
DR   Proteomes; UP000000607; 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..643
FT                   /note="Macrolide export ATP-binding/permease protein MacB"
FT                   /id="PRO_0000269946"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        523..543
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        572..592
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        603..623
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   DOMAIN          4..242
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   BINDING         40..47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ   SEQUENCE   643 AA;  69529 MW;  7A9AF8C63DB0DFA3 CRC64;
     MNIIEIKELN RYFGEGENTV HVLKNISVNI EKGDFVAIIG QSGSGKSTLM NIIGCLDTAT
     SGSYKIDGKE TNELTSDQLS DLRSQKFGFI FQRYNLLSAL TAAENVALPA IYAGKSQSER
     LARAEELLKK LGLDGKEKNK PSELSGGQQQ RVSIARALMN GGEIILADEP TGALDSHSGE
     NVLEILRQLH SEGHTIIMVT HDKNIAASAN RIIEIKDGEI IDDTQKHPVQ NTVNNQSKAK
     SRFGFSKDQL MEAFQMSVSA IIAHKMRSLL TMLGIIIGIT SVVSVVALGN GSQQKILSNI
     SGLGTNTMTI FNGTGFGDRR AEQMQNLTVN DANALAKQSY VQNVTPNSSS SGLLIYGNQS
     FTSTNLKGIG EQYFDVEGMT LKQGRSITAQ EVRDNAQVAL LDESSKKSIF PNDNPIDKIV
     MFAKRPFRII GVVADRQMGA ASSSLNIYAP YTTVMNKVTG GTKIDSITVK IADNVNTAVA
     EKSLTEYLTV RHGKKDFFIM NSDTIKQTIE STTGTMKLLI SSIAFISLIV GGIGVMNIML
     VSVTERTKEI GVRMAIGARK SNILQQFLIE AILICMIGGI SGIMLSLIIG GIFNVFMTDF
     TMVFSTFSIV AAVLCSTLIG VIFGYMPAKN AAQLDPITAL ARE
 
 
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