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Q5HGE8 (PGSA_STAAC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase

EC=2.7.8.5
Alternative name(s):
Phosphatidylglycerophosphate synthase
Short name=PGP synthase
Gene names
Name:pgsA
Ordered Locus Names:SACOL1302
OrganismStaphylococcus aureus (strain COL) [Complete proteome] [HAMAP]
Taxonomic identifier93062 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length192 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

This protein catalyzes the committed step to the synthesis of the acidic phospholipids By similarity.

Catalytic activity

CDP-diacylglycerol + sn-glycerol 3-phosphate = CMP + 3(3-sn-phosphatidyl)-sn-glycerol 1-phosphate.

Pathway

Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the CDP-alcohol phosphatidyltransferase class-I family.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processphospholipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionCDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 192192CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
PRO_0000056784

Regions

Transmembrane7 – 2923Helical; Potential
Transmembrane44 – 6320Helical; Potential
Transmembrane84 – 10623Helical; Potential
Transmembrane129 – 15123Helical; Potential
Transmembrane157 – 17923Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
Q5HGE8 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 9DE1A740E101C674

FASTA19221,014
        10         20         30         40         50         60 
MNIPNQITVF RVVLIPVFIL FALVDFGFGN VSFLGGYEIR IELLISGFIF ILASLSDFVD 

        70         80         90        100        110        120 
GYLARKWNLV TNMGKFLDPL ADKLLVASAL IVLVQLGLTN SVVAIIIIAR EFAVTGLRLL 

       130        140        150        160        170        180 
QIEQGFVSAA GQLGKIKTAV TMVAITWLLL GDPLATLIGL SLGQILLYIG VIFTILSGIE 

       190 
YFYKGRDVFK QK 

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: COL.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000046 Genomic DNA. Translation: AAW38133.1.
RefSeqYP_186159.1. NC_002951.2.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HGE8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000008977; EBSTAP00000008712; EBSTAG00000008976.
GeneID3236361.
GenomeReviewsGene locus SACOL1302 in contig CP000046_GR.
KEGGsac:SACOL1302.
PATRIC19528839. VBIStaAur112458_1272.
TIGRSACOL1302.

Phylogenomic databases

eggNOGCOG0558.
GeneTreeEBGT00050000025045.
HOGENOMHBG686655.
OMAWITIVIV.
PhylomeDBQ5HGE8.
ProtClustDBCLSK885249.

Enzyme and pathway databases

BioCycSAUR93062:SACOL1302-MONOMER.

Family and domain databases

InterProIPR000462. CDP-OH_P_trans.
IPR004570. Phosphatidylglycerol_P_synth.
[Graphical view]
KOK00995.
PfamPF01066. CDP-OH_P_transf. 1 hit.
[Graphical view]
PIRSFPIRSF000847. Phos_ph_gly_syn. 1 hit.
TIGRFAMsTIGR00560. PgsA. 1 hit.
PROSITEPS00379. CDP_ALCOHOL_P_TRANSF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGSA_STAAC
AccessionPrimary (citable) accession number: Q5HGE8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: February 15, 2005
Last modified: January 25, 2012
This is version 54 of the entry and version 1 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