PCRB_STAA8
ID PCRB_STAA8 Reviewed; 230 AA.
AC Q53726; Q2G1X8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 128.
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, ECO:0000269|PubMed:21761520, ECO:0000269|PubMed:24684232};
DE AltName: Full=Glycerol-1-phosphate heptaprenyltransferase {ECO:0000255|HAMAP-Rule:MF_00112};
GN Name=pcrB {ECO:0000255|HAMAP-Rule:MF_00112};
GN OrderedLocusNames=SAOUHSC_02124;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8232203; DOI=10.1007/bf00280216;
RA Iordanescu S.;
RT "Characterization of the Staphylococcus aureus chromosomal gene pcrA,
RT identified by mutations affecting plasmid pT181 replication.";
RL Mol. Gen. Genet. 241:185-192(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=21761520; DOI=10.1002/anie.201101832;
RA Guldan H., Matysik F.M., Bocola M., Sterner R., Babinger P.;
RT "Functional assignment of an enzyme that catalyzes the synthesis of an
RT archaea-type ether lipid in bacteria.";
RL Angew. Chem. Int. Ed. Engl. 50:8188-8191(2011).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=24684232; DOI=10.1111/mmi.12596;
RA Peterhoff D., Beer B., Rajendran C., Kumpula E.P., Kapetaniou E.,
RA Guldan H., Wierenga R.K., Sterner R., Babinger P.;
RT "A comprehensive analysis of the geranylgeranylglyceryl phosphate synthase
RT enzyme family identifies novel members and reveals mechanisms of substrate
RT specificity and quaternary structure organization.";
RL Mol. Microbiol. 92:885-899(2014).
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. To a much lesser extent, is also able to
CC use geranylgeranyl diphosphate (GGPP; C20) as the prenyl donor.
CC {ECO:0000269|PubMed:21761520, ECO:0000269|PubMed:24684232}.
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 ECO:0000269|PubMed:21761520, ECO:0000269|PubMed:24684232};
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 ECO:0000269|PubMed:21761520, ECO:0000269|PubMed:24684232}.
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; M63176; AAA72090.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD31173.1; -; Genomic_DNA.
DR PIR; S39922; S39922.
DR RefSeq; WP_000272070.1; NZ_LS483365.1.
DR RefSeq; YP_500615.1; NC_007795.1.
DR AlphaFoldDB; Q53726; -.
DR SMR; Q53726; -.
DR STRING; 1280.SAXN108_2006; -.
DR EnsemblBacteria; ABD31173; ABD31173; SAOUHSC_02124.
DR GeneID; 3921195; -.
DR KEGG; sao:SAOUHSC_02124; -.
DR PATRIC; fig|93061.5.peg.1927; -.
DR eggNOG; COG1646; Bacteria.
DR HOGENOM; CLU_095211_0_0_9; -.
DR OMA; TGAHKEW; -.
DR UniPathway; UPA00940; -.
DR PRO; PR:Q53726; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0002094; F:polyprenyltransferase activity; IGI:UniProtKB.
DR GO; GO:0004659; F:prenyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IGI:UniProtKB.
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 1: Evidence at protein level;
KW Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..230
FT /note="Heptaprenylglyceryl phosphate synthase"
FT /id="PRO_0000138722"
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 CONFLICT 218..230
FT /note="KALKTVKIKESSK -> SFKNSKNKGV (in Ref. 1; AAA72090)"
FT /evidence="ECO:0000305"
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
