UPPS_FRATT
ID UPPS_FRATT Reviewed; 257 AA.
AC Q5NHX6;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=FTT_0317;
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
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; AJ749949; CAG44950.1; -; Genomic_DNA.
DR RefSeq; YP_169366.1; NC_006570.2.
DR AlphaFoldDB; Q5NHX6; -.
DR SMR; Q5NHX6; -.
DR STRING; 177416.FTT_0317; -.
DR DNASU; 3191904; -.
DR EnsemblBacteria; CAG44950; CAG44950; FTT_0317.
DR KEGG; ftu:FTT_0317; -.
DR eggNOG; COG0020; Bacteria.
DR OMA; PRTEGHK; -.
DR Proteomes; UP000001174; 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; Reference proteome; Transferase.
FT CHAIN 1..257
FT /note="Ditrans,polycis-undecaprenyl-diphosphate synthase
FT ((2E,6E)-farnesyl-diphosphate specific)"
FT /id="PRO_0000123614"
FT ACT_SITE 34
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT ACT_SITE 82
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 34
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 35..38
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 47
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 207..209
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
SQ SEQUENCE 257 AA; 29706 MW; 780F911FECC1A057 CRC64;
MFILSYHLAN LIFFIIFMTS AKENILRHLA IIMDGNGRWA KSRLKPRIFG HRNSVSSVDA
TIEYCVENNI EMLTLFAFGR DNWLRPAQEV SDLMDLFYKT LKDKTPKLHD NNIVVTVVGD
RSRLSNKLIG MIEYSESLTK SNTGLKLRLA VDYAGRWDIV EATRAIAREV DIGKLSVDEI
DQNSFAKYLV GGNMPVDLLI RTSGEVRLSD FMLWQLAYAE MYFTDIMWPD FSKQELTRAV
EYFYSRQRRF GKSGEQI
