UPPS_PSEAE
ID UPPS_PSEAE Reviewed; 251 AA.
AC Q9HXY2;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, 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=PA3652;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP THEORETICAL MODEL.
RA Guo R.T., Kuo C.J., Chen C.L., Ko T.P., Liang P.H., Wang A.H.-J.;
RT "Comparative modeling for protein structure prediction of undecaprenyl
RT pyrophosphate synthetase upps form pseudomonas aeruginosa.";
RL Submitted (FEB-2009) to the PDB data bank.
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; AE004091; AAG07040.1; -; Genomic_DNA.
DR PIR; G83188; G83188.
DR RefSeq; NP_252342.1; NC_002516.2.
DR RefSeq; WP_003113863.1; NZ_QZGE01000001.1.
DR AlphaFoldDB; Q9HXY2; -.
DR SMR; Q9HXY2; -.
DR STRING; 287.DR97_4287; -.
DR BindingDB; Q9HXY2; -.
DR ChEMBL; CHEMBL4523935; -.
DR PaxDb; Q9HXY2; -.
DR PRIDE; Q9HXY2; -.
DR EnsemblBacteria; AAG07040; AAG07040; PA3652.
DR GeneID; 880553; -.
DR KEGG; pae:PA3652; -.
DR PATRIC; fig|208964.12.peg.3821; -.
DR PseudoCAP; PA3652; -.
DR HOGENOM; CLU_038505_1_1_6; -.
DR InParanoid; Q9HXY2; -.
DR OMA; PRTEGHK; -.
DR PhylomeDB; Q9HXY2; -.
DR BioCyc; PAER208964:G1FZ6-3722-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008834; F:di-trans,poly-cis-decaprenylcistransferase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IBA:GO_Central.
DR GO; GO:0002094; F:polyprenyltransferase activity; IBA:GO_Central.
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:0016094; P:polyprenol biosynthetic process; IBA:GO_Central.
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..251
FT /note="Ditrans,polycis-undecaprenyl-diphosphate synthase
FT ((2E,6E)-farnesyl-diphosphate specific)"
FT /id="PRO_0000123654"
FT ACT_SITE 19
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT ACT_SITE 67
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 19
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 20..23
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 24
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 64..66
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 193..195
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 206
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
SQ SEQUENCE 251 AA; 28040 MW; 3C30B4542C7A0016 CRC64;
MEKTRKDVCV PRHVAIIMDG NNRWAKKRLL PGVAGHKAGV DAVRAVIEVC AEAGVEVLTL
FAFSSENWQR PADEVSALME LFLVALRREV RKLDENGIRL RIIGDRTRFH PELQAAMREA
EAATAGNTRF LLQVAANYGG QWDIVQAAQR LAREVQGGHL AADDISAELL QGCLVTGDQP
LPDLCIRTGG EHRISNFLLW QLAYAELYFS DLFWPDFKHA AMRAALADFS KRQRRFGKTS
EQVEAEARPS C
