ID   PCRB_LYSSC              Reviewed;         229 AA.
AC   B1HTW4;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Heptaprenylglyceryl phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00112};
DE            Short=HepGP synthase {ECO:0000255|HAMAP-Rule:MF_00112};
DE            EC=2.5.1.n9 {ECO:0000255|HAMAP-Rule:MF_00112};
DE   AltName: Full=Glycerol-1-phosphate heptaprenyltransferase {ECO:0000255|HAMAP-Rule:MF_00112};
GN   Name=pcrB {ECO:0000255|HAMAP-Rule:MF_00112}; OrderedLocusNames=Bsph_0224;
OS   Lysinibacillus sphaericus (strain C3-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=444177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C3-41;
RX   PubMed=18296527; DOI=10.1128/jb.01652-07;
RA   Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA   Berry C., Yuan Z.;
RT   "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT   sphaericus C3-41 and comparison with those of closely related Bacillus
RT   species.";
RL   J. Bacteriol. 190:2892-2902(2008).
CC   -!- FUNCTION: Prenyltransferase that catalyzes in vivo the transfer of the
CC       heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon
CC       atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing
CC       heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond-
CC       formation step in the biosynthesis of archaea-type G1P-based membrane
CC       lipids found in Bacillales. {ECO:0000255|HAMAP-Rule:MF_00112}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-heptaprenyl diphosphate + sn-glycerol 1-phosphate =
CC         3-heptaprenyl-sn-glycero-1-phosphate + diphosphate;
CC         Xref=Rhea:RHEA:33495, ChEBI:CHEBI:33019, ChEBI:CHEBI:57685,
CC         ChEBI:CHEBI:58206, ChEBI:CHEBI:64781; EC=2.5.1.n9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00112};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00112};
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC       {ECO:0000255|HAMAP-Rule:MF_00112}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00112}.
CC   -!- SIMILARITY: Belongs to the GGGP/HepGP synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00112}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACA37855.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CP000817; ACA37855.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; B1HTW4; -.
DR   SMR; B1HTW4; -.
DR   EnsemblBacteria; ACA37855; ACA37855; Bsph_0224.
DR   KEGG; lsp:Bsph_0224; -.
DR   HOGENOM; CLU_095211_0_0_9; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000002164; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0002094; F:polyprenyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046474; P:glycerophospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02812; PcrB_like; 1.
DR   Gene3D; 3.20.20.390; -; 1.
DR   HAMAP; MF_00112; GGGP_HepGP_synthase; 1.
DR   InterPro; IPR039074; GGGP/HepGP_synthase_I.
DR   InterPro; IPR038597; GGGP/HepGP_synthase_sf.
DR   InterPro; IPR008205; GGGP_HepGP_synthase.
DR   PANTHER; PTHR40029; PTHR40029; 1.
DR   Pfam; PF01884; PcrB; 1.
DR   TIGRFAMs; TIGR01768; GGGP-family; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Transferase.
FT   CHAIN           1..229
FT                   /note="Heptaprenylglyceryl phosphate synthase"
FT                   /id="PRO_0000350671"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         39
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
SQ   SEQUENCE   229 AA;  25532 MW;  F2BBBC66D6EC617E CRC64;
     MDYLEWRHVF RLDPAKDISD EDLEKICESG TDVILVGGTD NVTLDGVLDL LVRVRRFEVP
     IALEISTIDA ITPGYDYYFI PTVLNSDDPK WIKNLHHAAI KEFGDIMVWD ELVAEGYCIL
     NPDCKVAHVT GATTDLSIDD IVAYARMAEN FFKLPVFYLE YSGIYGNPEV VSAVKNELKH
     TKLFYGGGIT SAKQAEEMAQ YADTVVVGNI IYEDLKAALA TVKAVKNTL