UniProtKB - P60472 (UPPS_ECOLI)
Protein
Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific)
Gene
ispU
Organism
Escherichia coli (strain K12)
Status
Functioni
Generates ditrans,octacis-undecaprenyl pyrophosphate (UPP) from isopentenyl pyrophosphate (IPP) and farnesyl diphosphate (FPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide.1 Publication
Catalytic activityi
- (2E,6E)-farnesyl diphosphate + 8 isopentenyl diphosphate = di-trans,octa-cis-undecaprenyl diphosphate + 8 diphosphateEC:2.5.1.31
Cofactori
Mg2+2 PublicationsNote: Binds 2 magnesium ions per subunit.2 Publications
Activity regulationi
Inhibited by bisphosphonates.1 Publication
Kineticsi
- KM=0.4 µM for FPP (at pH 7.5 and at 25 degrees Celsius)1 Publication
- KM=4.1 µM for IPP (at pH 7.5 and at 25 degrees Celsius)1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 26 | 1 | ||
Metal bindingi | 26 | Magnesium | 1 | |
Binding sitei | 31 | Substrate1 Publication | 1 | |
Binding sitei | 39 | Substrate1 Publication | 1 | |
Binding sitei | 43 | Substrate1 Publication | 1 | |
Sitei | 69 | Required for continued chain elongation | 1 | |
Active sitei | 74 | Proton acceptorBy similarity | 1 | |
Binding sitei | 75 | Substrate1 Publication | 1 | |
Binding sitei | 77 | Substrate1 Publication | 1 | |
Sitei | 137 | Important for determining product length | 1 | |
Binding sitei | 194 | Substrate1 Publication | 1 | |
Metal bindingi | 199 | Magnesium | 1 | |
Metal bindingi | 213 | Magnesium | 1 | |
Binding sitei | 213 | Isopentenyl diphosphate | 1 |
GO - Molecular functioni
- di-trans,poly-cis-decaprenylcistransferase activity Source: EcoCyc
- magnesium ion binding Source: EcoCyc
- manganese ion binding Source: GO_Central
- polyprenyltransferase activity Source: GO_Central
GO - Biological processi
- cell cycle Source: UniProtKB-KW
- cell division Source: UniProtKB-KW
- cell wall organization Source: UniProtKB-KW
- Gram-negative-bacterium-type cell wall biogenesis Source: EcoCyc
- peptidoglycan biosynthetic process Source: EcoCyc
- polyprenol biosynthetic process Source: EcoCyc
- regulation of cell shape Source: UniProtKB-KW
Keywordsi
Molecular function | Transferase |
Biological process | Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:UPPSYN-MONOMER MetaCyc:UPPSYN-MONOMER |
BRENDAi | 2.5.1.31, 2026 |
SABIO-RKi | P60472 |
Chemistry databases
SwissLipidsi | SLP:000001809 |
Names & Taxonomyi
Protein namesi | Recommended name: Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) (EC:2.5.1.31)Alternative name(s): Ditrans,polycis-undecaprenylcistransferase Undecaprenyl diphosphate synthase Short name: UDS Undecaprenyl pyrophosphate synthase Short name: UPP synthase |
Gene namesi | Name:ispU Synonyms:rth, uppS, yaeS Ordered Locus Names:b0174, JW0169 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
GO - Cellular componenti
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 26 | D → A: Great decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 31 | W → F: Decrease in activity; reduced affinity for decaprenyl diphosphate substrate analog. 1 Publication | 1 | |
Mutagenesisi | 43 | H → A: Great decreases in the catalytic efficiency and the affinity for FPP and IPP. 1 Publication | 1 | |
Mutagenesisi | 62 | I → A: Formation predominantly of C(60) and C(65) polymers rather than the C(55) polymer. 1 Publication | 1 | |
Mutagenesisi | 69 | A → L: Produces shorter polymers. 1 Publication | 1 | |
Mutagenesisi | 71 | S → A: Decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 73 | E → A: Slight decrease in activity. 2 Publications | 1 | |
Mutagenesisi | 74 | N → A: Decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 75 | W → A or F: Decrease in activity; reduced affinity for decaprenyl diphosphate substrate analog. 2 Publications | 1 | |
Mutagenesisi | 77 | R → A: Decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 81 | E → A: Slight decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 91 | W → F: Decrease in affinity for IPP. 1 Publication | 1 | |
Mutagenesisi | 103 | H → A: No effect. 1 Publication | 1 | |
Mutagenesisi | 105 | V → A: Formation predominantly of C(60), C(65) and C(70) polymers rather than the C(55) polymer. 1 Publication | 1 | |
Mutagenesisi | 137 | L → A: Formation predominantly of a C(70) polymer rather than the C(55) polymer. 1 Publication | 1 | |
Mutagenesisi | 143 | A → V: No effect on polymer length. 1 Publication | 1 | |
Mutagenesisi | 149 | W → F: Decrease in affinity for IPP. 1 Publication | 1 | |
Mutagenesisi | 150 | D → A: Great decrease in affinity for the substrate. 1 Publication | 1 | |
Mutagenesisi | 190 | D → A: No effect. 1 Publication | 1 | |
Mutagenesisi | 198 | E → A: No effect. 1 Publication | 1 | |
Mutagenesisi | 199 | H → A: Great decreases in the catalytic efficiency and in the affinity for IPP; when associated with A-213. 1 Publication | 1 | |
Mutagenesisi | 207 | W → F: Decrease in affinity for both IPP and decaprenyl diphosphate substrate analog. 1 Publication | 1 | |
Mutagenesisi | 213 | E → A: Great decrease in activity; reduced affinity for IPP. Great decreases in the catalytic efficiency and in the affinity for IPP; when associated with A-199. 2 Publications | 1 | |
Mutagenesisi | 218 | D → A: Slight decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 221 | W → F: Decrease in affinity for IPP. 1 Publication | 1 | |
Mutagenesisi | 223 | D → A: No effect. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL4295580 |
DrugBanki | DB07409, (1-HYDROXY-1-PHOSPHONO-2-[1,1';4',1'']TERPHENYL-3-YL-ETHYL)-PHOSPHONIC ACID DB07426, [1-HYDROXY-2-(1,1':3',1''-TERPHENYL-3-YLOXY)ETHANE-1,1-DIYL]BIS(PHOSPHONIC ACID) DB07410, [2-(3-DIBENZOFURAN-4-YL-PHENYL)-1-HYDROXY-1-PHOSPHONO-ETHYL]-PHOSPHONIC ACID DB07404, BPH-608 DB07780, Farnesyl diphosphate DB04695, Farnesyl thiopyrophosphate DB04714, ISOPENTENYL PYROPHOSPHATE |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000123609 | 1 – 253 | Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific)Add BLAST | 253 |
Proteomic databases
jPOSTi | P60472 |
PaxDbi | P60472 |
PRIDEi | P60472 |
Interactioni
Subunit structurei
Homodimer.
6 PublicationsProtein-protein interaction databases
BioGRIDi | 4260767, 417 interactors |
DIPi | DIP-48251N |
IntActi | P60472, 4 interactors |
STRINGi | 511145.b0174 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P60472 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P60472 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 26 – 30 | Substrate binding | 5 | |
Regioni | 71 – 73 | Substrate bindingBy similarity | 3 | |
Regioni | 200 – 202 | Substrate binding | 3 |
Sequence similaritiesi
Belongs to the UPP synthase family.Curated
Phylogenomic databases
eggNOGi | COG0020, Bacteria |
HOGENOMi | CLU_038505_1_1_6 |
InParanoidi | P60472 |
PhylomeDBi | P60472 |
Family and domain databases
CDDi | cd00475, Cis_IPPS, 1 hit |
DisProti | DP00516 |
Gene3Di | 3.40.1180.10, 1 hit |
HAMAPi | MF_01139, ISPT, 1 hit |
InterProi | View protein in InterPro IPR001441, UPP_synth-like IPR018520, UPP_synth-like_CS IPR036424, UPP_synth-like_sf |
PANTHERi | PTHR10291, PTHR10291, 1 hit |
Pfami | View protein in Pfam PF01255, Prenyltransf, 1 hit |
SUPFAMi | SSF64005, SSF64005, 1 hit |
TIGRFAMsi | TIGR00055, uppS, 1 hit |
PROSITEi | View protein in PROSITE PS01066, UPP_SYNTHASE, 1 hit |
i Sequence
Sequence statusi: Complete.
P60472-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MMLSATQPLS EKLPAHGCRH VAIIMDGNGR WAKKQGKIRA FGHKAGAKSV
60 70 80 90 100
RRAVSFAANN GIEALTLYAF SSENWNRPAQ EVSALMELFV WALDSEVKSL
110 120 130 140 150
HRHNVRLRII GDTSRFNSRL QERIRKSEAL TAGNTGLTLN IAANYGGRWD
160 170 180 190 200
IVQGVRQLAE KVQQGNLQPD QIDEEMLNQH VCMHELAPVD LVIRTGGEHR
210 220 230 240 250
ISNFLLWQIA YAELYFTDVL WPDFDEQDFE GALNAFANRE RRFGGTEPGD
ETA
Sequence cautioni
The sequence AAB08603 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U70214 Genomic DNA Translation: AAB08603.1 Different initiation. U00096 Genomic DNA Translation: AAC73285.1 AP009048 Genomic DNA Translation: BAA77849.2 |
PIRi | F64741 |
RefSeqi | NP_414716.1, NC_000913.3 |
Genome annotation databases
EnsemblBacteriai | AAC73285; AAC73285; b0174 BAA77849; BAA77849; BAA77849 |
GeneIDi | 944874 |
KEGGi | ecj:JW0169 eco:b0174 |
PATRICi | fig|511145.12.peg.180 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U70214 Genomic DNA Translation: AAB08603.1 Different initiation. U00096 Genomic DNA Translation: AAC73285.1 AP009048 Genomic DNA Translation: BAA77849.2 |
PIRi | F64741 |
RefSeqi | NP_414716.1, NC_000913.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1JP3 | X-ray | 1.80 | A/B | 1-253 | [»] | |
1UEH | X-ray | 1.73 | A/B | 1-253 | [»] | |
1V7U | X-ray | 2.35 | A/B | 1-253 | [»] | |
1X06 | X-ray | 1.90 | A | 1-253 | [»] | |
1X07 | X-ray | 2.20 | A | 1-253 | [»] | |
1X08 | X-ray | 1.90 | A | 1-253 | [»] | |
1X09 | X-ray | 1.87 | A | 1-253 | [»] | |
2E98 | X-ray | 1.90 | A/B | 1-253 | [»] | |
2E99 | X-ray | 2.00 | A/B | 1-253 | [»] | |
2E9A | X-ray | 2.10 | A/B | 1-253 | [»] | |
2E9C | X-ray | 2.05 | A/B | 1-253 | [»] | |
2E9D | X-ray | 2.50 | A/B | 1-253 | [»] | |
3QAS | X-ray | 1.70 | A/B | 1-253 | [»] | |
3SGV | X-ray | 1.61 | A/B | 1-253 | [»] | |
3SGX | X-ray | 2.45 | A/B | 1-253 | [»] | |
3SH0 | X-ray | 1.84 | A/B | 1-253 | [»] | |
3TH8 | X-ray | 2.11 | A/B | 1-253 | [»] | |
3WYJ | X-ray | 2.10 | A/B | 1-253 | [»] | |
4H2J | X-ray | 1.81 | A/B | 1-253 | [»] | |
4H2M | X-ray | 1.78 | A/B | 1-253 | [»] | |
4H2O | X-ray | 2.14 | A/B | 1-253 | [»] | |
4H38 | X-ray | 1.95 | A/B | 1-253 | [»] | |
4H3A | X-ray | 1.98 | A/B | 1-253 | [»] | |
4H3C | X-ray | 1.93 | A/B | 1-253 | [»] | |
5CQB | X-ray | 2.20 | A/B | 2-253 | [»] | |
5CQJ | X-ray | 2.15 | A/B | 1-253 | [»] | |
5ZHE | X-ray | 2.18 | A/B | 1-253 | [»] | |
SMRi | P60472 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4260767, 417 interactors |
DIPi | DIP-48251N |
IntActi | P60472, 4 interactors |
STRINGi | 511145.b0174 |
Chemistry databases
ChEMBLi | CHEMBL4295580 |
DrugBanki | DB07409, (1-HYDROXY-1-PHOSPHONO-2-[1,1';4',1'']TERPHENYL-3-YL-ETHYL)-PHOSPHONIC ACID DB07426, [1-HYDROXY-2-(1,1':3',1''-TERPHENYL-3-YLOXY)ETHANE-1,1-DIYL]BIS(PHOSPHONIC ACID) DB07410, [2-(3-DIBENZOFURAN-4-YL-PHENYL)-1-HYDROXY-1-PHOSPHONO-ETHYL]-PHOSPHONIC ACID DB07404, BPH-608 DB07780, Farnesyl diphosphate DB04695, Farnesyl thiopyrophosphate DB04714, ISOPENTENYL PYROPHOSPHATE |
SwissLipidsi | SLP:000001809 |
Proteomic databases
jPOSTi | P60472 |
PaxDbi | P60472 |
PRIDEi | P60472 |
Genome annotation databases
EnsemblBacteriai | AAC73285; AAC73285; b0174 BAA77849; BAA77849; BAA77849 |
GeneIDi | 944874 |
KEGGi | ecj:JW0169 eco:b0174 |
PATRICi | fig|511145.12.peg.180 |
Organism-specific databases
EchoBASEi | EB3113 |
Phylogenomic databases
eggNOGi | COG0020, Bacteria |
HOGENOMi | CLU_038505_1_1_6 |
InParanoidi | P60472 |
PhylomeDBi | P60472 |
Enzyme and pathway databases
BioCyci | EcoCyc:UPPSYN-MONOMER MetaCyc:UPPSYN-MONOMER |
BRENDAi | 2.5.1.31, 2026 |
SABIO-RKi | P60472 |
Miscellaneous databases
EvolutionaryTracei | P60472 |
PROi | PR:P60472 |
Family and domain databases
CDDi | cd00475, Cis_IPPS, 1 hit |
DisProti | DP00516 |
Gene3Di | 3.40.1180.10, 1 hit |
HAMAPi | MF_01139, ISPT, 1 hit |
InterProi | View protein in InterPro IPR001441, UPP_synth-like IPR018520, UPP_synth-like_CS IPR036424, UPP_synth-like_sf |
PANTHERi | PTHR10291, PTHR10291, 1 hit |
Pfami | View protein in Pfam PF01255, Prenyltransf, 1 hit |
SUPFAMi | SSF64005, SSF64005, 1 hit |
TIGRFAMsi | TIGR00055, uppS, 1 hit |
PROSITEi | View protein in PROSITE PS01066, UPP_SYNTHASE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | UPPS_ECOLI | |
Accessioni | P60472Primary (citable) accession number: P60472 Secondary accession number(s): P75668, Q47675, Q9R2E4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 16, 2004 |
Last sequence update: | February 16, 2004 | |
Last modified: | December 2, 2020 | |
This is version 146 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families