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Q53726 (PCRB_STAA8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Heptaprenylglyceryl phosphate synthase

Short name=HepGP synthase
EC=2.5.1.n9
Alternative name(s):
Glycerol-1-phosphate heptaprenyltransferase
Gene names
Name:pcrB
Ordered Locus Names:SAOUHSC_02124
OrganismStaphylococcus aureus (strain NCTC 8325) [Reference proteome] [HAMAP]
Taxonomic identifier93061 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length230 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 geranylgeranyl diphosphate (GGPP; C20) as the prenyl donor. Ref.3

Catalytic activity

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

Cofactor

Magnesium By similarity.

Pathway

Membrane lipid metabolism; glycerophospholipid metabolism. HAMAP-Rule MF_00112

Subunit structure

Homodimer. Ref.3

Sequence similarities

Belongs to the GGGP/HepGP synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 230230Heptaprenylglyceryl phosphate synthase HAMAP-Rule MF_00112
PRO_0000138722

Regions

Region159 – 1613Glycerol-1-phosphate binding By similarity

Sites

Metal binding141Magnesium Potential
Metal binding401Magnesium Potential
Binding site121Glycerol-1-phosphate By similarity
Binding site1641Glycerol-1-phosphate; via amide nitrogen By similarity
Binding site1891Glycerol-1-phosphate; via amide nitrogen By similarity
Binding site2101Glycerol-1-phosphate By similarity

Experimental info

Sequence conflict218 – 23013KALKT…KESSK → SFKNSKNKGV in AAA72090. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q53726 [UniParc].

Last modified June 27, 2006. Version 2.
Checksum: B1C76CDE9A23E702

FASTA23025,889
        10         20         30         40         50         60 
MYDIKKWRHI FKLDPAKHIS DDDLDAICMS QTDAIMIGGT DDVTEDNVIH LMSRVRRYPL 

        70         80         90        100        110        120 
PLVLEISNIE SVMPGFDFYF VPTVLNSTDV VFHNGTLLEA LKTYGHSIDF EEVIFEGYVV 

       130        140        150        160        170        180 
CNADSKVAKH TKANTDLTTE DLEAYAQMVN HMYRLPVMYI EYSGIYGDVS KVQAVSEHLT 

       190        200        210        220        230 
ETQLFYGGGI SSEQQATEMA AIADTIIVGD IIYKDIKKAL KTVKIKESSK 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the Staphylococcus aureus chromosomal gene pcrA, identified by mutations affecting plasmid pT181 replication."
Iordanescu S.
Mol. Gen. Genet. 241:185-192(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The Staphylococcus aureus NCTC8325 genome."
Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 8325.
[3]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63176 Genomic DNA. Translation: AAA72090.1.
CP000253 Genomic DNA. Translation: ABD31173.1.
PIRS39922.
RefSeqYP_500615.1. NC_007795.1.

3D structure databases

ProteinModelPortalQ53726.
SMRQ53726. Positions 1-225.
ModBaseSearch...

Protein-protein interaction databases

STRING93061.SAOUHSC_02124.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD31173; ABD31173; SAOUHSC_02124.
GeneID3921195.
KEGGsao:SAOUHSC_02124.
PATRIC19581611. VBIStaAur99865_1927.

Phylogenomic databases

eggNOGCOG1646.
HOGENOMHOG000015607.
KOK07094.
OMAYLEYSGV.
ProtClustDBPRK04169.

Enzyme and pathway databases

BioCycSAUR93061:GIWJ-2068-MONOMER.
UniPathwayUPA00940.

Family and domain databases

Gene3D3.20.20.390. 1 hit.
HAMAPMF_00112. GGGP_HepGP_synthase.
InterProIPR008205. GGGP_HepGP_synthase.
[Graphical view]
PfamPF01884. PcrB. 1 hit.
[Graphical view]
TIGRFAMsTIGR01768. GGGP-family. 1 hit.
ProtoNetSearch...

Entry information

Entry namePCRB_STAA8
AccessionPrimary (citable) accession number: Q53726
Secondary accession number(s): Q2G1X8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 27, 2006
Last modified: May 1, 2013
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families