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UPPS_BUCAP
ID   UPPS_BUCAP              Reviewed;         249 AA.
AC   Q8K9S6;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) {ECO:0000255|HAMAP-Rule:MF_01139};
DE            EC=2.5.1.31 {ECO:0000255|HAMAP-Rule:MF_01139};
DE   AltName: Full=Ditrans,polycis-undecaprenylcistransferase {ECO:0000255|HAMAP-Rule:MF_01139};
DE   AltName: Full=Undecaprenyl diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_01139};
DE            Short=UDS {ECO:0000255|HAMAP-Rule:MF_01139};
DE   AltName: Full=Undecaprenyl pyrophosphate synthase {ECO:0000255|HAMAP-Rule:MF_01139};
DE            Short=UPP synthase {ECO:0000255|HAMAP-Rule:MF_01139};
GN   Name=uppS {ECO:0000255|HAMAP-Rule:MF_01139}; OrderedLocusNames=BUsg_230;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- FUNCTION: Catalyzes the sequential condensation of isopentenyl
CC       diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield
CC       (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di-
CC       trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in
CC       the biosynthesis of bacterial cell wall polysaccharide components such
CC       as peptidoglycan and lipopolysaccharide. {ECO:0000255|HAMAP-
CC       Rule:MF_01139}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = di-
CC         trans,octa-cis-undecaprenyl diphosphate + 8 diphosphate;
CC         Xref=Rhea:RHEA:27551, ChEBI:CHEBI:33019, ChEBI:CHEBI:58405,
CC         ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.31;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01139};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01139};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01139};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01139}.
CC   -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01139}.
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DR   EMBL; AE013218; AAM67789.1; -; Genomic_DNA.
DR   RefSeq; WP_011053756.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9S6; -.
DR   SMR; Q8K9S6; -.
DR   STRING; 198804.BUsg_230; -.
DR   EnsemblBacteria; AAM67789; AAM67789; BUsg_230.
DR   KEGG; bas:BUsg_230; -.
DR   eggNOG; COG0020; Bacteria.
DR   HOGENOM; CLU_038505_1_1_6; -.
DR   OMA; PRTEGHK; -.
DR   OrthoDB; 1630604at2; -.
DR   Proteomes; UP000000416; Chromosome.
DR   GO; GO:0008834; F:di-trans,poly-cis-decaprenylcistransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   CDD; cd00475; Cis_IPPS; 1.
DR   Gene3D; 3.40.1180.10; -; 1.
DR   HAMAP; MF_01139; ISPT; 1.
DR   InterPro; IPR001441; UPP_synth-like.
DR   InterPro; IPR018520; UPP_synth-like_CS.
DR   InterPro; IPR036424; UPP_synth-like_sf.
DR   PANTHER; PTHR10291; PTHR10291; 1.
DR   Pfam; PF01255; Prenyltransf; 1.
DR   SUPFAM; SSF64005; SSF64005; 1.
DR   TIGRFAMs; TIGR00055; uppS; 1.
DR   PROSITE; PS01066; UPP_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Cell shape; Cell wall biogenesis/degradation; Magnesium; Metal-binding;
KW   Peptidoglycan synthesis; Transferase.
FT   CHAIN           1..249
FT                   /note="Ditrans,polycis-undecaprenyl-diphosphate synthase
FT                   ((2E,6E)-farnesyl-diphosphate specific)"
FT                   /id="PRO_0000123585"
FT   ACT_SITE        26
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   ACT_SITE        74
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         26
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         27..30
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         31
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         43
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         71..73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         200..202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT   BINDING         213
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
SQ   SEQUENCE   249 AA;  29601 MW;  6EC8CFE3AA7A8197 CRC64;
     MLYKSSLKNK KRIQKENLRH IAIIMDGNGR WAEKRGKIRT LGHKEGFKTA RKIIKYAVEN
     NIKILTLYVF SRENWRRPKL EITALMKLFF FALKSEIKNL NKYNIRLKII GDTSPFNENL
     KNYIHKVEKQ TFNNTGLILN IAANYSGRWD IIRGIKKIIK DVQKDVLDID QIQERNFSQY
     LSTSELLPVD LVIRTGGEKR ISNFLLWQIA YSELYFTDIL WPDFNWRDFQ HAIDYFFTRE
     RRFGGISIS
 
 
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