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Protein

Heptaprenylglyceryl phosphate synthase

Gene

pcrB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond-formation step in the biosynthesis of archaea-type G1P-based membrane lipids found in Bacillales. To a much lesser extent, is also able to use geranyl diphosphate (GPP; C10) and geranylgeranyl diphosphate (GGPP; C20) as the prenyl donors, but not farnesyl pyrophosphate (FPP; C15). Cannot use glycerol-3-phosphate (G3P) or 3-phosphoglycerate (3PG) as an acceptor.3 Publications

Catalytic activityi

All-trans-heptaprenyl diphosphate + sn-glycerol 1-phosphate = diphosphate + sn-3-O-(all-trans-heptaprenyl)glycerol 1-phosphate.UniRule annotation2 Publications

Cofactori

Mg2+UniRule annotation

Pathwayi: glycerophospholipid metabolism

This protein is involved in the pathway glycerophospholipid metabolism, which is part of Membrane lipid metabolism.UniRule annotation1 Publication
View all proteins of this organism that are known to be involved in the pathway glycerophospholipid metabolism and in Membrane lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei12Glycerol-1-phosphateUniRule annotationCombined sources1 Publication1
Metal bindingi14MagnesiumUniRule annotation1
Metal bindingi40MagnesiumUniRule annotation1
Binding sitei188Glycerol-1-phosphate; via amide nitrogenUniRule annotationCombined sources1 Publication1

GO - Molecular functioni

GO - Biological processi

  • glycerophospholipid biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU06600-MONOMER.
UniPathwayiUPA00940.

Names & Taxonomyi

Protein namesi
Recommended name:
Heptaprenylglyceryl phosphate synthaseUniRule annotationCurated (EC:2.5.1.n9UniRule annotation2 Publications)
Short name:
HepGP synthaseUniRule annotationCurated
Alternative name(s):
Glycerol-1-phosphate heptaprenyltransferaseUniRule annotationCurated
Gene namesi
Name:pcrBUniRule annotation
Synonyms:yerE
Ordered Locus Names:BSU06600
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene show a cloggy growth and do not produce the dephosphorylated and acetylated derivatives of HepGP.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001387111 – 228Heptaprenylglyceryl phosphate synthaseAdd BLAST228

Proteomic databases

PaxDbiO34790.

Interactioni

Subunit structurei

Homodimer.UniRule annotation3 Publications

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100003733.

Structurei

Secondary structure

1228
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 6Combined sources3
Beta strandi9 – 13Combined sources5
Helixi23 – 28Combined sources6
Beta strandi33 – 37Combined sources5
Beta strandi40 – 42Combined sources3
Helixi45 – 55Combined sources11
Beta strandi58 – 60Combined sources3
Beta strandi62 – 65Combined sources4
Helixi69 – 71Combined sources3
Beta strandi77 – 84Combined sources8
Beta strandi87 – 89Combined sources3
Turni90 – 94Combined sources5
Helixi95 – 110Combined sources16
Beta strandi113 – 120Combined sources8
Beta strandi123 – 125Combined sources3
Helixi126 – 130Combined sources5
Helixi139 – 151Combined sources13
Beta strandi155 – 160Combined sources6
Helixi168 – 177Combined sources10
Beta strandi179 – 188Combined sources10
Helixi192 – 199Combined sources8
Beta strandi203 – 207Combined sources5
Helixi210 – 213Combined sources4
Helixi215 – 219Combined sources5
Helixi221 – 226Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VIZX-ray1.85A/B2-228[»]
3VZXX-ray1.54A/B1-228[»]
3VZYX-ray1.63A/B1-228[»]
3VZZX-ray2.04A/B1-228[»]
3W00X-ray2.50A/B1-228[»]
ProteinModelPortaliO34790.
SMRiO34790.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO34790.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni158 – 163Glycerol-1-phosphate bindingUniRule annotationCombined sources1 Publication6
Regioni208 – 209Glycerol-1-phosphate bindingUniRule annotationCombined sources1 Publication2

Sequence similaritiesi

Belongs to the GGGP/HepGP synthase family. Group I subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108RTE. Bacteria.
COG1646. LUCA.
HOGENOMiHOG000015607.
InParanoidiO34790.
KOiK07094.
OMAiDPAKEIS.
PhylomeDBiO34790.

Family and domain databases

CDDicd02812. PcrB_like. 1 hit.
Gene3Di3.20.20.390. 1 hit.
HAMAPiMF_00112. GGGP_HepGP_synthase. 1 hit.
InterProiIPR008205. GGGP_HepGP_synthase.
[Graphical view]
PfamiPF01884. PcrB. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01768. GGGP-family. 1 hit.

Sequencei

Sequence statusi: Complete.

O34790-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYDVTEWKHV FKLDPNKDLP DEQLEILCES GTDAVIIGGS DGVTEDNVLR
60 70 80 90 100
MMSKVRRFLV PCVLEVSAIE AIVPGFDLYF IPSVLNSKNA DWIVGMHQKA
110 120 130 140 150
MKEYGELMSM EEIVAEGYCI ANPDCKAAAL TEADADLNMD DIVAYARVSE
160 170 180 190 200
LLQLPIFYLE YSGVLGDIEA VKKTKAVLET STLFYGGGIK DAETAKQYAE
210 220
HADVIVVGNA VYEDFDRALK TVAAVKGE
Length:228
Mass (Da):25,088
Last modified:January 1, 1998 - v1
Checksum:i05360F1F863A5ABA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y15254 Genomic DNA. Translation: CAA75551.1.
AL009126 Genomic DNA. Translation: CAB12480.1.
PIRiD69794.
RefSeqiNP_388542.1. NC_000964.3.
WP_003233922.1. NZ_JNCM01000032.1.

Genome annotation databases

EnsemblBacteriaiCAB12480; CAB12480; BSU06600.
GeneIDi936052.
KEGGibsu:BSU06600.
PATRICi18972966. VBIBacSub10457_0697.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y15254 Genomic DNA. Translation: CAA75551.1.
AL009126 Genomic DNA. Translation: CAB12480.1.
PIRiD69794.
RefSeqiNP_388542.1. NC_000964.3.
WP_003233922.1. NZ_JNCM01000032.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VIZX-ray1.85A/B2-228[»]
3VZXX-ray1.54A/B1-228[»]
3VZYX-ray1.63A/B1-228[»]
3VZZX-ray2.04A/B1-228[»]
3W00X-ray2.50A/B1-228[»]
ProteinModelPortaliO34790.
SMRiO34790.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100003733.

Proteomic databases

PaxDbiO34790.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12480; CAB12480; BSU06600.
GeneIDi936052.
KEGGibsu:BSU06600.
PATRICi18972966. VBIBacSub10457_0697.

Phylogenomic databases

eggNOGiENOG4108RTE. Bacteria.
COG1646. LUCA.
HOGENOMiHOG000015607.
InParanoidiO34790.
KOiK07094.
OMAiDPAKEIS.
PhylomeDBiO34790.

Enzyme and pathway databases

UniPathwayiUPA00940.
BioCyciBSUB:BSU06600-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO34790.

Family and domain databases

CDDicd02812. PcrB_like. 1 hit.
Gene3Di3.20.20.390. 1 hit.
HAMAPiMF_00112. GGGP_HepGP_synthase. 1 hit.
InterProiIPR008205. GGGP_HepGP_synthase.
[Graphical view]
PfamiPF01884. PcrB. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01768. GGGP-family. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPCRB_BACSU
AccessioniPrimary (citable) accession number: O34790
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: November 30, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The HepGP product, which is the first archaea-type G1P-based ether lipid being identified within the phylogenetic domain of the bacteria, was found to be subsequently dephosphorylated and acetylated in vivo. However, HepG and its acetylated derivatives represent only a minor fraction of the total lipid in B.subtilis.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.