Q53726 (PCRB_STAA8) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Staphylococcus aureus (strain NCTC 8325) [Reference proteome] [HAMAP]

Taxonomic identifier

93061 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus aureus › Staphylococcus aureus subsp. aureus

Protein attributes

Sequence length	230 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Ligand	Magnesium Metal-binding
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycerophospholipid biosynthetic process Inferred from genetic interaction Ref.3. Source: UniProtKB
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP polyprenyltransferase activity Inferred from genetic interaction Ref.3. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 230	230	Heptaprenylglyceryl phosphate synthase HAMAP-Rule MF_00112		PRO_0000138722
Regions
	Region	159 – 161	3	Glycerol-1-phosphate binding By similarity
Sites
	Metal binding	14	1	Magnesium Potential
	Metal binding	40	1	Magnesium Potential
	Binding site	12	1	Glycerol-1-phosphate By similarity
	Binding site	164	1	Glycerol-1-phosphate; via amide nitrogen By similarity
	Binding site	189	1	Glycerol-1-phosphate; via amide nitrogen By similarity
	Binding site	210	1	Glycerol-1-phosphate By similarity
Experimental info
	Sequence conflict	218 – 230	13	KALKT…KESSK → SFKNSKNKGV in AAA72090. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q53726 [UniParc]. Last modified June 27, 2006. Version 2. Checksum: B1C76CDE9A23E702	FASTA	230	25,889
	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

References

	« Hide 'large scale' referencesShow '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.
PIR	S39922.
RefSeq	YP_500615.1. NC_007795.1.
3D structure databases
ProteinModelPortal	Q53726.
SMR	Q53726. Positions 1-225.
ModBase	Search...
Protein-protein interaction databases
STRING	93061.SAOUHSC_02124.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABD31173; ABD31173; SAOUHSC_02124.
GeneID	3921195.
KEGG	sao:SAOUHSC_02124.
PATRIC	19581611. VBIStaAur99865_1927.
Phylogenomic databases
eggNOG	COG1646.
HOGENOM	HOG000015607.
KO	K07094.
OMA	YLEYSGV.
ProtClustDB	PRK04169.
Enzyme and pathway databases
BioCyc	SAUR93061:GIWJ-2068-MONOMER.
UniPathway	UPA00940.
Family and domain databases
Gene3D	3.20.20.390. 1 hit.
HAMAP	MF_00112. GGGP_HepGP_synthase.
InterPro	IPR008205. GGGP_HepGP_synthase. [Graphical view]
Pfam	PF01884. PcrB. 1 hit. [Graphical view]
TIGRFAMs	TIGR01768. GGGP-family. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PCRB_STAA8

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program