ID A0A084IK12_SALHC Unreviewed; 240 AA.
AC A0A084IK12;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ORFNames=C41B8_12040 {ECO:0000313|EMBL:KEZ77046.1};
OS Salinisphaera hydrothermalis (strain C41B8).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Salinisphaerales;
OC Salinisphaeraceae; Salinisphaera.
OX NCBI_TaxID=1304275 {ECO:0000313|EMBL:KEZ77046.1, ECO:0000313|Proteomes:UP000028302};
RN [1] {ECO:0000313|EMBL:KEZ77046.1, ECO:0000313|Proteomes:UP000028302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C41B8 {ECO:0000313|EMBL:KEZ77046.1,
RC ECO:0000313|Proteomes:UP000028302};
RA Li C., Lai Q., Shao Z.;
RT "Salinisphaera hydrothermalis C41B8 Genome Sequencing.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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;
CC Evidence={ECO:0000256|HAMAP-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEZ77046.1}.
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DR EMBL; APNK01000018; KEZ77046.1; -; Genomic_DNA.
DR RefSeq; WP_037338481.1; NZ_APNK01000018.1.
DR AlphaFoldDB; A0A084IK12; -.
DR STRING; 1304275.C41B8_12040; -.
DR PATRIC; fig|1304275.5.peg.2456; -.
DR eggNOG; COG0020; Bacteria.
DR OrthoDB; 4191603at2; -.
DR Proteomes; UP000028302; Unassembled WGS sequence.
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:UP000028302};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01139}.
FT ACT_SITE 13
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT ACT_SITE 61
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 14..17
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 26
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 58..60
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 187..189
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
FT BINDING 200
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01139"
SQ SEQUENCE 240 AA; 26767 MW; A52B376E2D5D44D3 CRC64;
MSSTPKHVAV IMDGNGRWAS GRGLPRAAGH RAGAKIAHEI VESASKAGVG TLTLFAFSSE
NWKRPRPEVR LLMDLLRRTI RKELASLDAN NVRMHFIGDR TRFSAALANE MKAAEERTAS
NTGLRLLIAV DYGGRWDIVR RTRELAAACG RGELEADDIT EEQFSEGLSL GPFGPPDLFI
RTGGERRISN FLLWDLAYSE LYFTDVLWPD FGPDRLYDAL DWYAGRERRF GSLVAPAAQR
//
