(data stored in SCRATCH zone)

SWISSPROT: D3UWG4_XENBS

ID   D3UWG4_XENBS            Unreviewed;       231 AA.
AC   D3UWG4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   16-JAN-2019, entry version 52.
DE   RecName: Full=Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) {ECO:0000256|HAMAP-Rule:MF_01139};
DE            EC=2.5.1.31 {ECO:0000256|HAMAP-Rule:MF_01139};
DE   AltName: Full=Ditrans,polycis-undecaprenylcistransferase {ECO:0000256|HAMAP-Rule:MF_01139};
DE   AltName: Full=Undecaprenyl diphosphate synthase {ECO:0000256|HAMAP-Rule:MF_01139};
DE            Short=UDS {ECO:0000256|HAMAP-Rule:MF_01139};
DE   AltName: Full=Undecaprenyl pyrophosphate synthase {ECO:0000256|HAMAP-Rule:MF_01139};
DE            Short=UPP synthase {ECO:0000256|HAMAP-Rule:MF_01139};
GN   Name=ispU {ECO:0000313|EMBL:CBJ79738.1};
GN   Synonyms=uppS {ECO:0000256|HAMAP-Rule:MF_01139};
GN   OrderedLocusNames=XBJ1_0594 {ECO:0000313|EMBL:CBJ79738.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79738.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79738.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79738.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Catalyzes the sequential condensation of isopentenyl
CC       diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to
CC       yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl
CC       diphosphate (di-trans,octa-cis-UPP). UPP is the precursor of
CC       glycosyl carrier lipid in the biosynthesis of bacterial cell wall
CC       polysaccharide components such as peptidoglycan and
CC       lipopolysaccharide. {ECO:0000256|HAMAP-Rule:MF_01139}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate
CC         = di-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:0000256|HAMAP-Rule:MF_01139};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01139};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01139};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01139}.
CC   -!- SIMILARITY: Belongs to the UPP synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01139}.
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DR   EMBL; FN667741; CBJ79738.1; -; Genomic_DNA.
DR   STRING; 406818.XBJ1_0594; -.
DR   EnsemblBacteria; CBJ79738; CBJ79738; XBJ1_0594.
DR   KEGG; xbo:XBJ1_0594; -.
DR   eggNOG; ENOG4105CR3; Bacteria.
DR   eggNOG; COG0020; LUCA.
DR   HOGENOM; HOG000006054; -.
DR   KO; K00806; -.
DR   OMA; FDRRDLW; -.
DR   Proteomes; UP000002045; 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;
DR   PRODOM; D3UWG4.
DR   SWISS-2DPAGE; D3UWG4.
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_01139};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_01139};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01139};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01139};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_01139};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01139,
KW   ECO:0000313|EMBL:CBJ79738.1}.
FT   REGION        3      6       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01139}.
FT   REGION       47     49       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01139}.
FT   REGION      176    178       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01139}.
FT   ACT_SITE      2      2       {ECO:0000256|HAMAP-Rule:MF_01139}.
FT   ACT_SITE     50     50       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01139}.
FT   METAL         2      2       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01139}.
FT   METAL       175    175       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01139}.
FT   METAL       189    189       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01139}.
FT   BINDING       7      7       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01139}.
FT   BINDING      15     15       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01139}.
FT   BINDING      19     19       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01139}.
FT   BINDING      51     51       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01139}.
FT   BINDING      53     53       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01139}.
FT   BINDING     170    170       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01139}.
SQ   SEQUENCE   231 AA;  26061 MW;  7E45B9119A3716F3 CRC64;
     MDGNGRWAKQ RGKLRVFGHR AGVKAVRVAV SFSVKHNIES LTLYAFSSEN WNRPQQEVSS
     LMELFVFALD NEVKSLHKHN VKLSVIGDIS RFSSRLQERI RRSVELTAGN TGLQLNIAAN
     YGGRWDLVQG VKQIAEKIRA NELEPEEITE ATVGSVINLS EQPEVDLVIR TGGEHRISNF
     LLWQIAYAEL YFTDILWPDF DETVFEGAIN AFVKRERRFG GTIPDDAEVG S
//

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