UPPS_LACPL
ID UPPS_LACPL Reviewed; 259 AA.
AC Q88VJ8; F9UQ06;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific);
DE EC=2.5.1.31;
DE AltName: Full=Ditrans,polycis-undecaprenylcistransferase;
DE AltName: Full=Undecaprenyl diphosphate synthase;
DE Short=UDS;
DE AltName: Full=Undecaprenyl pyrophosphate synthase;
DE Short=UPP synthase;
GN Name=uppS; OrderedLocusNames=lp_2051;
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
RN [3]
RP FUNCTION AS AN UNDECAPRENYL DIPHOSPHATE SYNTHASE, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=6712246; DOI=10.1016/0003-9861(84)90085-7;
RA Muth J.D., Allen C.M.;
RT "Undecaprenyl pyrophosphate synthetase from Lactobacillus plantarum: a
RT dimeric protein.";
RL Arch. Biochem. Biophys. 230:49-60(1984).
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:0000269|PubMed:6712246}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.13 uM for FPP {ECO:0000269|PubMed:6712246};
CC KM=1.93 uM for IPP {ECO:0000269|PubMed:6712246};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:6712246}.
CC -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
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DR EMBL; AL935263; CCC79295.1; -; Genomic_DNA.
DR RefSeq; WP_003640735.1; NC_004567.2.
DR RefSeq; YP_004889809.1; NC_004567.2.
DR AlphaFoldDB; Q88VJ8; -.
DR SMR; Q88VJ8; -.
DR STRING; 220668.lp_2051; -.
DR EnsemblBacteria; CCC79295; CCC79295; lp_2051.
DR GeneID; 57025601; -.
DR KEGG; lpl:lp_2051; -.
DR PATRIC; fig|220668.9.peg.1736; -.
DR eggNOG; COG0020; Bacteria.
DR HOGENOM; CLU_038505_1_1_9; -.
DR OMA; PRTEGHK; -.
DR PhylomeDB; Q88VJ8; -.
DR BioCyc; LPLA220668:G1GW0-1756-MON; -.
DR BRENDA; 2.5.1.31; 2849.
DR SABIO-RK; Q88VJ8; -.
DR Proteomes; UP000000432; Chromosome.
DR GO; GO:0008834; F:di-trans,poly-cis-decaprenylcistransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
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 1: Evidence at protein level;
KW Magnesium; Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..259
FT /note="Ditrans,polycis-undecaprenyl-diphosphate synthase
FT ((2E,6E)-farnesyl-diphosphate specific)"
FT /id="PRO_0000123628"
FT ACT_SITE 32
FT /evidence="ECO:0000250"
FT ACT_SITE 80
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 32
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 33..36
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 77..79
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 209..211
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 259 AA; 28838 MW; 243B4658138B8323 CRC64;
MFAFFNKNDP ADNTDVQLDP ERIPAHVAII MDGNGRWAKA RHLPRVAGHK EGMNTVKKIT
IAASDLGVKV LTLYAFSTEN WKRPTDEVNY LMQLPVSFFD TFVPDLIKNN VRVQVMGYVD
HLPEATQKAV QNAIADTKDC DGMVLNFALN YGSRAEIVTG VQKIAQQVQD GQLAVGDIDD
ATIDAALMTA PLAPYNDPDL LIRTSGEERI SNFLMWQIAY SELVFTDVKW PDFTAATLQA
CIADFQSRDR RFGGLSDHK
