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Protein

Heptaprenylglyceryl phosphate synthase

Gene

pcrB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 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.2 Publications

Catalytic activityi

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

Cofactori

Mg2+By similarity

Pathwayi: glycerophospholipid metabolism

This protein is involved in the pathway glycerophospholipid metabolism, which is part of Membrane lipid metabolism.1 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei12 – 121Glycerol-1-phosphateBy similarity
Metal bindingi14 – 141MagnesiumSequence analysis
Metal bindingi40 – 401MagnesiumSequence analysis
Binding sitei163 – 1631Glycerol-1-phosphate; via amide nitrogenBy similarity
Binding sitei188 – 1881Glycerol-1-phosphate; via amide nitrogenBy similarity
Binding sitei209 – 2091Glycerol-1-phosphateBy similarity

GO - Molecular functioni

  • magnesium ion binding Source: UniProtKB-HAMAP
  • polyprenyltransferase activity Source: UniProtKB

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 synthase (EC:2.5.1.n9)
Short name:
HepGP synthase
Alternative name(s):
Glycerol-1-phosphate heptaprenyltransferase
Gene namesi
Name:pcrB
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 228228Heptaprenylglyceryl phosphate synthasePRO_0000138711Add
BLAST

Proteomic databases

PaxDbiO34790.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100003733.

Structurei

Secondary structure

1
228
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 63Combined sources
Beta strandi9 – 135Combined sources
Helixi23 – 286Combined sources
Beta strandi33 – 375Combined sources
Beta strandi40 – 423Combined sources
Helixi45 – 5511Combined sources
Beta strandi58 – 603Combined sources
Beta strandi62 – 654Combined sources
Helixi69 – 713Combined sources
Beta strandi77 – 848Combined sources
Beta strandi87 – 893Combined sources
Turni90 – 945Combined sources
Helixi95 – 11016Combined sources
Beta strandi113 – 1208Combined sources
Beta strandi123 – 1253Combined sources
Helixi126 – 1305Combined sources
Helixi139 – 15113Combined sources
Beta strandi155 – 1606Combined sources
Helixi168 – 17710Combined sources
Beta strandi179 – 18810Combined sources
Helixi192 – 1998Combined sources
Beta strandi203 – 2075Combined sources
Helixi210 – 2134Combined sources
Helixi215 – 2195Combined sources
Helixi221 – 2266Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-228.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO34790.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni158 – 1603Glycerol-1-phosphate bindingBy similarity

Sequence similaritiesi

Belongs to the GGGP/HepGP synthase family.Curated

Phylogenomic databases

eggNOGiENOG4108RTE. Bacteria.
COG1646. LUCA.
HOGENOMiHOG000015607.
InParanoidiO34790.
KOiK07094.
OMAiDPAKEIS.
OrthoDBiEOG6XM79M.
PhylomeDBiO34790.

Family and domain databases

Gene3Di3.20.20.390. 1 hit.
HAMAPiMF_00112. GGGP_HepGP_synthase.
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
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. Positions 1-228.
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.
OrthoDBiEOG6XM79M.
PhylomeDBiO34790.

Enzyme and pathway databases

UniPathwayiUPA00940.
BioCyciBSUB:BSU06600-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO34790.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "PcrA is an essential DNA helicase of Bacillus subtilis fulfilling functions both in repair and rolling-circle replication."
    Petit M.-A., Dervyn E., Rose M., Entian K.-D., McGovern S., Ehrlich S.D., Bruand C.
    Mol. Microbiol. 29:261-273(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Identification and characterization of a bacterial glycerol-1-phosphate dehydrogenase: Ni(2+)-dependent AraM from Bacillus subtilis."
    Guldan H., Sterner R., Babinger P.
    Biochemistry 47:7376-7384(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PUTATIVE FUNCTION.
    Strain: 168.
  4. "Functional assignment of an enzyme that catalyzes the synthesis of an archaea-type ether lipid in bacteria."
    Guldan H., Matysik F.M., Bocola M., Sterner R., Babinger P.
    Angew. Chem. Int. Ed. Engl. 50:8188-8191(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBUNIT, PATHWAY, DISRUPTION PHENOTYPE.
    Strain: 168.
  5. "Two distinct mechanisms for TIM barrel prenyltransferases in bacteria."
    Doud E.H., Perlstein D.L., Wolpert M., Cane D.E., Walker S.
    J. Am. Chem. Soc. 133:1270-1273(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A PRENYLTRANSFERASE, STEREOCHEMISTRY, SUBSTRATE SPECIFICITY.
    Strain: 168 / PY79.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-228.

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: June 8, 2016
This is version 117 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.