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Reviewed, UniProtKB/Swiss-Prot Q5HGH0 (CDSA_STAAC)

Last modified November 3, 2009. Version 32. 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:
    Phosphatidate cytidylyltransferase
    EC=2.7.7.41
Alternative name(s):
    CDP-diglyceride pyrophosphorylase
    CDP-diglyceride synthetase
    CDP-diacylglycerol synthase
      Short name=CDS
    CTP:phosphatidate cytidylyltransferase
    CDP-DG synthetase
    CDP-DAG synthase
Gene names
Name: cdsA
Ordered Locus Names: SACOL1280
OrganismStaphylococcus aureus (strain COL) [Complete proteome] [HAMAP]
Taxonomic identifier93062 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length260 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

CTP + phosphatidate = diphosphate + CDP-diacylglycerol.

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the CDS family.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
   Molecular functionNucleotidyltransferase
Transferase
   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 functionphosphatidate cytidylyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 260260Phosphatidate cytidylyltransferase
PRO_0000090747

Regions

Transmembrane9 – 2921 Potential
Transmembrane46 – 6621 Potential
Transmembrane70 – 9021 Potential
Transmembrane102 – 12221 Potential
Transmembrane130 – 15021 Potential
Transmembrane172 – 19221 Potential
Transmembrane196 – 21621 Potential

Sequences

Sequence LengthMass (Da)Tools
Q5HGH0-1 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 02C2727C3801C694

FASTA26028,964
        10         20         30         40         50         60 
MKVRTLTAII ALIVFLPILL KGGLVLMIFA NILALIALKE LLNMNMIKFV SVPGLISAVG 

        70         80         90        100        110        120 
LIIIMLPQHA GPWVQVIQLK SLIAMSFIVL SYTVLSKNRF SFMDAAFCLM SVAYVGIGFM 

       130        140        150        160        170        180 
FFYETRSEGL HYILYAFLIV WLTDTGAYLF GKMMGKHKLW PVISPNKTIE GFIGGLFCSL 

       190        200        210        220        230        240 
IVPLAMLYFV DFNMNVWILL GVTLILSLFG QLGDLVESGF KRHFGVKDSG RILPGHGGIL 

       250        260 
DRFDSFMFVL PLLNILLIQS 

« 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

CP000046 Genomic DNA. Translation: AAW38111.1.
RefSeqYP_186137.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HGH0.

Genome annotation databases

GeneID3238386.
GenomeReviewsGene locus SACOL1280 in contig CP000046_GR.
KEGGsac:SACOL1280.
TIGRSACOL1280.

Phylogenomic databases

HOGENOMQ5HGH0.
OMASRNRFSF.

Enzyme and pathway databases

BioCycSAUR93062:SACOL1280-MON.

Family and domain databases

InterProIPR000374. PC_trans.
[Graphical view]
PfamPF01148. CTP_transf_1. 1 hit.
[Graphical view]
PROSITEPS01315. CDS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCDSA_STAAC
AccessionPrimary (citable) accession number: Q5HGH0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: February 15, 2005
Last modified: November 3, 2009
This is version 32 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