UPPS_BLOFL
ID UPPS_BLOFL Reviewed; 250 AA.
AC Q7VRE1;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=Bfl276;
OS Blochmannia floridanus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX NCBI_TaxID=203907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B.,
RA van Ham R.C.H.J., Gross R., Moya A.;
RT "The genome sequence of Blochmannia floridanus: comparative analysis of
RT reduced genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
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; BX248583; CAD83347.1; -; Genomic_DNA.
DR RefSeq; WP_011126556.1; NC_005061.1.
DR AlphaFoldDB; Q7VRE1; -.
DR SMR; Q7VRE1; -.
DR STRING; 203907.Bfl276; -.
DR EnsemblBacteria; CAD83347; CAD83347; Bfl276.
DR KEGG; bfl:Bfl276; -.
DR eggNOG; COG0020; Bacteria.
DR HOGENOM; CLU_038505_1_1_6; -.
DR OMA; PRTEGHK; -.
DR OrthoDB; 1630604at2; -.
DR Proteomes; UP000002192; 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..250
FT /note="Ditrans,polycis-undecaprenyl-diphosphate synthase
FT ((2E,6E)-farnesyl-diphosphate specific)"
FT /id="PRO_0000123589"
FT ACT_SITE 27
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT ACT_SITE 75
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 27
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 28..31
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 72..74
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 76
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 200
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 201..203
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
SQ SEQUENCE 250 AA; 28779 MW; F6A3D59ECB8EADAE CRC64;
MILSQFDQNI QPLSSAILPR HIAIIMDGNG RWARGRGKLR IVGHQAGFQA ARRAVRFAVH
CRFNALTLYA FSSENWTRSN TEISSLMQLF IYALNSEINN LNKNNIKLRI IGDVNRFTQE
LQDCIYRSEQ LTSNNNGLNL NIAANYGGRW DIVQGVKKII AQIQKGVLKP NQINENILCK
YVCMNELSPV DLVIRTGGEH RISNFLLWQI AYAELFFTDV LWPDFNDIVF RRALHSFMKR
DRRFGKSAFI
