ID UPPS_BUCAI Reviewed; 251 AA. AC P57330; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 27-MAR-2024, entry version 118. 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=BU236; OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon OS pisum symbiotic bacterium). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=107806; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=APS; RX PubMed=10993077; DOI=10.1038/35024074; RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.; RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera RT sp. APS."; RL Nature 407:81-86(2000). 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; Evidence={ECO:0000255|HAMAP- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000003; BAB12951.1; -; Genomic_DNA. DR RefSeq; NP_240065.1; NC_002528.1. DR RefSeq; WP_010896019.1; NC_002528.1. DR AlphaFoldDB; P57330; -. DR SMR; P57330; -. DR STRING; 563178.BUAP5A_231; -. DR EnsemblBacteria; BAB12951; BAB12951; BAB12951. DR KEGG; buc:BU236; -. DR PATRIC; fig|107806.10.peg.249; -. DR eggNOG; COG0020; Bacteria. DR HOGENOM; CLU_038505_1_1_6; -. DR Proteomes; UP000001806; 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; Decaprenyl diphosphate synthase-like; 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 NCBIfam; TIGR00055; uppS; 1. DR PANTHER; PTHR10291; DEHYDRODOLICHYL DIPHOSPHATE SYNTHASE FAMILY MEMBER; 1. DR PANTHER; PTHR10291:SF48; DITRANS,POLYCIS-UNDECAPRENYL-DIPHOSPHATE SYNTHASE ((2E,6E)-FARNESYL-DIPHOSPHATE SPECIFIC); 1. DR Pfam; PF01255; Prenyltransf; 1. DR SUPFAM; SSF64005; Undecaprenyl diphosphate synthase; 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_0000123584" FT ACT_SITE 26 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139" FT ACT_SITE 74 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139" FT BINDING 26 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139" FT BINDING 27..30 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139" FT BINDING 31 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 43 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139" FT BINDING 71..73 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139" FT BINDING 75 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139" FT BINDING 77 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139" FT BINDING 194 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139" FT BINDING 200..202 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139" FT BINDING 213 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139" SQ SEQUENCE 251 AA; 29381 MW; 5DEF9628012A88F5 CRC64; MQYKYLLEYN KKNHECNPCH VAIIMDGNGR WATRQGKIRI MGHKEGFRAV KEAIKFSIAN NLKILTLYAF SSENWNRPLF EIKALMELFL FALDTEIKNL KKHNIRFKVI GDITCFDKKL QNSIHYAEQI TFDNTGLILN IAANYGGRWD IIESVKKIIN RVQRGILDVN KIHENTISQY LSTSELLPVD LVIRTGGEKR ISNFLLWQIA YSELYFTDVL WPDFNCHIFQ HAIDSFVSRE RRFGGFKKNK K //