ID PCRB_STAA1 Reviewed; 230 AA.
AC A7X435;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
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=SAHV_1891;
OS Staphylococcus aureus (strain Mu3 / ATCC 700698).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=418127;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu3 / ATCC 700698;
RX PubMed=17954695; DOI=10.1128/aac.00534-07;
RA Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.;
RT "Mutated response regulator graR is responsible for phenotypic conversion
RT of Staphylococcus aureus from heterogeneous vancomycin-intermediate
RT resistance to vancomycin-intermediate resistance.";
RL Antimicrob. Agents Chemother. 52:45-53(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; AP009324; BAF78774.1; -; Genomic_DNA.
DR RefSeq; WP_000272054.1; NC_009782.1.
DR PDB; 3W01; X-ray; 1.54 A; A/B=1-230.
DR PDB; 3W02; X-ray; 2.98 A; A/B=1-230.
DR PDBsum; 3W01; -.
DR PDBsum; 3W02; -.
DR AlphaFoldDB; A7X435; -.
DR SMR; A7X435; -.
DR KEGG; saw:SAHV_1891; -.
DR HOGENOM; CLU_095211_0_0_9; -.
DR UniPathway; UPA00940; -.
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; FMN-linked oxidoreductases; 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 NCBIfam; TIGR01768; GGGP-family; 1.
DR PANTHER; PTHR40029; -; 1.
DR PANTHER; PTHR40029:SF2; HEPTAPRENYLGLYCERYL PHOSPHATE SYNTHASE; 1.
DR Pfam; PF01884; PcrB; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW Metal-binding; Phospholipid biosynthesis; Phospholipid metabolism;
KW Transferase.
FT CHAIN 1..230
FT /note="Heptaprenylglyceryl phosphate synthase"
FT /id="PRO_1000015168"
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"
FT HELIX 1..5
FT /evidence="ECO:0007829|PDB:3W01"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:3W01"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:3W01"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:3W01"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:3W01"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:3W01"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:3W02"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:3W01"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:3W01"
FT TURN 90..94
FT /evidence="ECO:0007829|PDB:3W01"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:3W01"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:3W01"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:3W01"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:3W01"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:3W01"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:3W01"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:3W01"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:3W01"
FT HELIX 169..176
FT /evidence="ECO:0007829|PDB:3W01"
FT STRAND 180..188
FT /evidence="ECO:0007829|PDB:3W01"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:3W01"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:3W01"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:3W01"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:3W01"
SQ SEQUENCE 230 AA; 25847 MW; 9027D26A586E84FC CRC64;
MYDIKKWRHI FKLDPAKHIS DDDLDAICMS QTDAIMIGGT DDVTEDNVIH LMSKIRRYPL
PLVLEISNIE SVMPGFDFYF VPTVLNSTDV AFHNGTLLEA LKTYGHSIDF EEVIFEGYVV
CNADSKVAKH TKANTDLTTE DLEAYAQMVN HMYRLPVMYI EYSGIYGDVS KVQAVSEHLT
ETQLFYGGGI SSEQQATEMA AIADTIIVGD IIYKDIKKAL KTVKIKESSK
//
