ID   PCRB_STAAE              Reviewed;         230 AA.
AC   A6QID4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=NWMN_1844;
OS   Staphylococcus aureus (strain Newman).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=426430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Newman;
RX   PubMed=17951380; DOI=10.1128/jb.01000-07;
RA   Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT   "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT   analysis of staphylococcal genomes: polymorphism and evolution of two major
RT   pathogenicity islands.";
RL   J. Bacteriol. 190:300-310(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. Group I
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00112}.
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DR   EMBL; AP009351; BAF68116.1; -; Genomic_DNA.
DR   RefSeq; WP_000272070.1; NZ_CP023390.1.
DR   AlphaFoldDB; A6QID4; -.
DR   SMR; A6QID4; -.
DR   EnsemblBacteria; BAF68116; BAF68116; NWMN_1844.
DR   KEGG; sae:NWMN_1844; -.
DR   HOGENOM; CLU_095211_0_0_9; -.
DR   OMA; TGAHKEW; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000006386; 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..230
FT                   /note="Heptaprenylglyceryl phosphate synthase"
FT                   /id="PRO_1000071334"
FT   BINDING         12
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         14
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         40
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         159..164
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         189
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         209..210
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
SQ   SEQUENCE   230 AA;  25889 MW;  B1C76CDE9A23E702 CRC64;
     MYDIKKWRHI FKLDPAKHIS DDDLDAICMS QTDAIMIGGT DDVTEDNVIH LMSRVRRYPL
     PLVLEISNIE SVMPGFDFYF VPTVLNSTDV VFHNGTLLEA LKTYGHSIDF EEVIFEGYVV
     CNADSKVAKH TKANTDLTTE DLEAYAQMVN HMYRLPVMYI EYSGIYGDVS KVQAVSEHLT
     ETQLFYGGGI SSEQQATEMA AIADTIIVGD IIYKDIKKAL KTVKIKESSK