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Reviewed, UniProtKB/Swiss-Prot Q5HPQ8 (PGSA_STAEQ)

Last modified February 9, 2010. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: SERP0850
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length193 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
   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-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 193193CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
PRO_0000056791

Regions

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

Sequences

Sequence LengthMass (Da)Tools
Q5HPQ8-1 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: B59344586D41B319

FASTA19321,497
        10         20         30         40         50         60 
MNIPNQITVF RVILIPFFIL FALVDFGFGQ ISILGGNHIR IEILISAIIF VVASLSDFAD 

        70         80         90        100        110        120 
GYLARKWQLV TNMGKFLDPL ADKLLVASAL IVMVQLGFTN SVVAIIIIAR EFAVTGLRLL 

       130        140        150        160        170        180 
QIEQGFVSAA GQLGKIKTAV TMVAIIWILL GDPFVHYLRF PIGVWLLYIG VFFTILSGIE 

       190 
YFYKGRDVFK HSK 

« 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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000029 Genomic DNA. Translation: AAW54227.1.
RefSeqYP_188432.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HPQ8.

Genome annotation databases

GeneID3242631.
GenomeReviewsGene locus SERP0850 in contig CP000029_GR.
KEGGser:SERP0850.
TIGRSERP0850.

Phylogenomic databases

eggNOGCOG0558.
HOGENOMHBG686655.
OMAYLARKWE.

Enzyme and pathway databases

BioCycSEPI176279:SERP0850-MONOMER.

Family and domain databases

InterProIPR000462. CDP-OH_P_trans.
IPR004570. Phosphatidylglycerol_P_synth.
[Graphical view]
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_STAEQ
AccessionPrimary (citable) accession number: Q5HPQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: February 15, 2005
Last modified: February 9, 2010
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents