ID A7MGS7_CROS8 Unreviewed; 252 AA. AC A7MGS7; DT 02-OCT-2007, integrated into UniProtKB/TrEMBL. DT 02-OCT-2007, sequence version 1. DT 27-MAR-2024, entry version 92. DE RecName: Full=Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) {ECO:0000256|HAMAP-Rule:MF_01139}; DE EC=2.5.1.31 {ECO:0000256|HAMAP-Rule:MF_01139}; DE AltName: Full=Ditrans,polycis-undecaprenylcistransferase {ECO:0000256|HAMAP-Rule:MF_01139}; DE AltName: Full=Undecaprenyl diphosphate synthase {ECO:0000256|HAMAP-Rule:MF_01139}; DE Short=UDS {ECO:0000256|HAMAP-Rule:MF_01139}; DE AltName: Full=Undecaprenyl pyrophosphate synthase {ECO:0000256|HAMAP-Rule:MF_01139}; DE Short=UPP synthase {ECO:0000256|HAMAP-Rule:MF_01139}; GN Name=uppS {ECO:0000256|HAMAP-Rule:MF_01139}; GN OrderedLocusNames=ESA_03168 {ECO:0000313|EMBL:ABU78391.1}; OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Cronobacter. OX NCBI_TaxID=290339 {ECO:0000313|EMBL:ABU78391.1, ECO:0000313|Proteomes:UP000000260}; RN [1] {ECO:0000313|EMBL:ABU78391.1, ECO:0000313|Proteomes:UP000000260} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-894 {ECO:0000313|EMBL:ABU78391.1, RC ECO:0000313|Proteomes:UP000000260}; RX PubMed=20221447; DOI=10.1371/journal.pone.0009556; RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L., RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A., RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K., RA McClelland M., Forsythe S.J.; RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic RT hybridization analysis with other Cronobacter species."; RL PLoS ONE 5:E9556-E9556(2010). 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:0000256|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:0000256|HAMAP-Rule:MF_01139}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01139}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01139}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP- CC Rule:MF_01139}. CC -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000256|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; CP000783; ABU78391.1; -; Genomic_DNA. DR RefSeq; WP_004386134.1; NC_009778.1. DR AlphaFoldDB; A7MGS7; -. DR GeneID; 56731859; -. DR KEGG; esa:ESA_03168; -. DR HOGENOM; CLU_038505_1_1_6; -. DR Proteomes; UP000000260; 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 {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP- KW Rule:MF_01139}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316, KW ECO:0000256|HAMAP-Rule:MF_01139}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01139}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01139}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP- KW Rule:MF_01139}; Reference proteome {ECO:0000313|Proteomes:UP000000260}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01139}. FT ACT_SITE 25 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139" FT ACT_SITE 73 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139" FT BINDING 25 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139" FT BINDING 26..29 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139" FT BINDING 30 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139" FT BINDING 38 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139" FT BINDING 42 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139" FT BINDING 70..72 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139" FT BINDING 74 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139" FT BINDING 76 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139" FT BINDING 193 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139" FT BINDING 198 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139" FT BINDING 199..201 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139" FT BINDING 212 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139" SQ SEQUENCE 252 AA; 28187 MW; 0434C816186E1178 CRC64; MLSVNLPLSE NLPAHGARHV AIIMDGNGRW AKRQGKIRAF GHKAGAKSVR RAVSFAANNG IEALTLYAFS SENWNRPAQE VSALMELFVW ALDSEVKSLH RHNVRLRVIG DISRFNTRLQ DRIHKAEALT SQNTGLTLNI AANYGGRWDI IQGVQQLAAQ VQEGLLRPDQ IDEEMLSKQI CMHELAPVDL VIRTGGEHRI SNFLLWQIAY AELYFTDVLW PDFDEQDFEG ALNAFANRER RFGGTAPGGI DA //