ID A0A1X7FX60_9BACI Unreviewed; 228 AA.
AC A0A1X7FX60; A0A0H4KBI5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Heptaprenylglyceryl phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00112};
DE Short=HepGP synthase {ECO:0000256|HAMAP-Rule:MF_00112};
DE EC=2.5.1.n9 {ECO:0000256|HAMAP-Rule:MF_00112};
DE AltName: Full=Glycerol-1-phosphate heptaprenyltransferase {ECO:0000256|HAMAP-Rule:MF_00112};
GN Name=pcrB {ECO:0000256|HAMAP-Rule:MF_00112};
GN ORFNames=B1B01_20280 {ECO:0000313|EMBL:OXS66320.1}, BEH_01925
GN {ECO:0000313|EMBL:AKO90985.1}, CJ485_13190
GN {ECO:0000313|EMBL:RJS65658.1}, SAMN06296056_106205
GN {ECO:0000313|EMBL:SMF60353.1};
OS Priestia filamentosa.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=1402861 {ECO:0000313|EMBL:SMF60353.1, ECO:0000313|Proteomes:UP000192915};
RN [1] {ECO:0000313|EMBL:AKO90985.1, ECO:0000313|Proteomes:UP000036202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hbe603 {ECO:0000313|EMBL:AKO90985.1,
RC ECO:0000313|Proteomes:UP000036202};
RX PubMed=26248285;
RA Jia N., Du J., Ding M.Z., Gao F., Yuan Y.J.;
RT "Genome Sequence of Bacillus endophyticus and Analysis of Its Companion
RT Mechanism in the Ketogulonigenium vulgare-Bacillus Strain Consortium.";
RL PLoS ONE 10:E0135104-E0135104(2015).
RN [2] {ECO:0000313|Proteomes:UP000036202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hbe603 {ECO:0000313|Proteomes:UP000036202};
RA Jia N., Du J., Ding M.-Z., Gao F., Yuan Y.-J.;
RT "Genome Sequence of Bacillus endophyticus and Analysis of its Companion
RT Mechanism in the Ketogulonigenium vulgare-Bacillus strain Consortium.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AKO90985.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Hbe603 {ECO:0000313|EMBL:AKO90985.1};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000215399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27955 {ECO:0000313|Proteomes:UP000215399};
RA Dastager S.G., Neurgaonkar P.S., Dharne M.S.;
RT "Bacillus sp. V-88(T) DSM27956, whole genome shotgun sequencing project.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|Proteomes:UP000192915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGD-14 {ECO:0000313|Proteomes:UP000192915};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:SMF60353.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27955 {ECO:0000313|EMBL:OXS66320.1}, and SGD-14
RC {ECO:0000313|EMBL:SMF60353.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:RJS65658.1, ECO:0000313|Proteomes:UP000274910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PK5_39 {ECO:0000313|EMBL:RJS65658.1,
RC ECO:0000313|Proteomes:UP000274910};
RA Bokhari A., Bougouffa S., Essack M., Andres-Barrao C., Saad M., Bajic V.B.,
RA Hirt H.;
RT "Complete genomes of four Endophytic plant-growth promoting Bacillus that
RT were isolated from a desert in Pakistan.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00001875, ECO:0000256|HAMAP-
CC Rule:MF_00112};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00112};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC {ECO:0000256|HAMAP-Rule:MF_00112}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00112}.
CC -!- SIMILARITY: Belongs to the GGGP/HepGP synthase family. Group I
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00112}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00112}.
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DR EMBL; CP011974; AKO90985.1; -; Genomic_DNA.
DR EMBL; MWSI01000006; OXS66320.1; -; Genomic_DNA.
DR EMBL; NQYF01000001; RJS65658.1; -; Genomic_DNA.
DR EMBL; FXAJ01000006; SMF60353.1; -; Genomic_DNA.
DR RefSeq; WP_040060841.1; NZ_NQYF01000001.1.
DR AlphaFoldDB; A0A1X7FX60; -.
DR KEGG; beo:BEH_01925; -.
DR PATRIC; fig|135735.6.peg.341; -.
DR eggNOG; COG1646; Bacteria.
DR OrthoDB; 2381757at2; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000036202; Chromosome.
DR Proteomes; UP000192915; Unassembled WGS sequence.
DR Proteomes; UP000215399; Unassembled WGS sequence.
DR Proteomes; UP000274910; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_00112};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_00112};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00112};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00112};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|HAMAP-Rule:MF_00112};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW Rule:MF_00112}; Reference proteome {ECO:0000313|Proteomes:UP000036202};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00112}.
FT BINDING 12
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT BINDING 14
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT BINDING 159..164
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT BINDING 189
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
FT BINDING 209..210
FT /ligand="sn-glycerol 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:57685"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00112"
SQ SEQUENCE 228 AA; 25122 MW; 6157A852E2C44209 CRC64;
MYDINGWKHV FKLDPNKDIS DEHLEQVCES GTDAIIVGGT DGVTLDNVLQ LLARIRRYTV
PCALEVSSID SVTPGFDFYF IPTVLNSSNT DFITGLHHQA MKEFGEIMDW NEIFVEGYCI
VNSDCKAAHV TEAKTELDEE DVIAYAQMAE RMFRLPIFYL EYSGVYGDVS LVKNVKNALS
TTKLFYGGGI ASSEQAVEMA HAADTVVVGN VIYEDLKAAL QTVGAVKG
//
