ID   PCRB_LISW6              Reviewed;         225 AA.
AC   A0AJL3;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=lwe1777;
OS   Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CIP 8149 /
OS   NCTC 11857 / SLCC 5334 / V8).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=386043;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35897 / DSM 20650 / CIP 8149 / NCTC 11857 / SLCC 5334 / V8;
RX   PubMed=16936040; DOI=10.1128/jb.00758-06;
RA   Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S.,
RA   Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O.,
RA   Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.,
RA   Lampidis R., Kreft J., Goebel W., Chakraborty T.;
RT   "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT   genome reduction with Listeria innocua as compared to Listeria
RT   monocytogenes.";
RL   J. Bacteriol. 188:7405-7415(2006).
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}.
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; AM263198; CAK21195.1; -; Genomic_DNA.
DR   RefSeq; WP_011702555.1; NC_008555.1.
DR   AlphaFoldDB; A0AJL3; -.
DR   SMR; A0AJL3; -.
DR   STRING; 386043.lwe1777; -.
DR   EnsemblBacteria; CAK21195; CAK21195; lwe1777.
DR   GeneID; 61189676; -.
DR   KEGG; lwe:lwe1777; -.
DR   eggNOG; COG1646; Bacteria.
DR   HOGENOM; CLU_095211_0_0_9; -.
DR   OMA; TGAHKEW; -.
DR   OrthoDB; 1439634at2; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000000779; 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..225
FT                   /note="Heptaprenylglyceryl phosphate synthase"
FT                   /id="PRO_0000350670"
FT   BINDING         6
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         34
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         153..158
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         183
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
FT   BINDING         203..204
FT                   /ligand="sn-glycerol 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57685"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00112"
SQ   SEQUENCE   225 AA;  25356 MW;  570CBC95B22CCB2A CRC64;
     MKHLFKLDPA KNLPHNSVTR LIHSGTDGFI IGGTDNLQTE AVENLYELLA ETDLPIFLEV
     SDESMILPEA EHFLIPVVLN TENSKWTHGL HKELIKEMGE FIPWKRVTSE GYVILNKDAK
     VAQLTEAKTD LTEEDIIAYA RLAENIFRLP IFYIEYSGMY GNPEVAKKVS AALDDTKFWY
     GGGIRSKEQA AEMAEYADTI IVGNIIYEDI EKALETTTVF AKKTV