PCRB_LISMO
ID PCRB_LISMO Reviewed; 225 AA.
AC Q8Y6C8;
DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 99.
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}; OrderedLocusNames=lmo1760;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
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 [3]
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}.
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DR EMBL; AL591981; CAC99838.1; -; Genomic_DNA.
DR PIR; AH1294; AH1294.
DR RefSeq; NP_465285.1; NC_003210.1.
DR RefSeq; WP_009930607.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y6C8; -.
DR SMR; Q8Y6C8; -.
DR STRING; 169963.lmo1760; -.
DR PaxDb; Q8Y6C8; -.
DR EnsemblBacteria; CAC99838; CAC99838; CAC99838.
DR GeneID; 985989; -.
DR KEGG; lmo:lmo1760; -.
DR PATRIC; fig|169963.11.peg.1804; -.
DR eggNOG; COG1646; Bacteria.
DR HOGENOM; CLU_095211_0_0_9; -.
DR OMA; TGAHKEW; -.
DR PhylomeDB; Q8Y6C8; -.
DR BioCyc; LMON169963:LMO1760-MON; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000000817; 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..225
FT /note="Heptaprenylglyceryl phosphate synthase"
FT /id="PRO_0000138715"
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; 25360 MW; 80EAEB841E8A638F CRC64;
MKHLFKLDPA KNLPTNDVTK LIHSGTDGFI IGGTDNVQIE AVQNLYELLV ETDLPIFLEI
SNESMILPEA DHFLIPVVLN TENSKWTHGL HKELIKEMGE FIPWKRVTSE GYVILNKDAK
VAHLTEAKTD LTDEDIVAYA RLAENIFHLP IFYVEYSGMY GDPEVVRKAS AALSNTKFWY
GGGIRSKEQA AEMAKYADTI IVGNIIYEDL EKALETATIF RKKTV
