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O31752 (CDSA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphatidate cytidylyltransferase
EC=2.7.7.41
Alternative name(s):
CDP-DAG synthase
CDP-DG synthase
CDP-diacylglycerol synthase
Short name=CDS
CDP-diglyceride pyrophosphorylase
CDP-diglyceride synthase
CTP:phosphatidate cytidylyltransferase
Gene names
Name:cdsA
Ordered Locus Names:BSU16540
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length269 AA.
Sequence statusComplete.
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
Transmembrane helix
   Molecular functionNucleotidyltransferase
Transferase
   Technical termComplete proteome
Reference 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 functionphosphatidate cytidylyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 269269Phosphatidate cytidylyltransferase
PRO_0000090726

Regions

Transmembrane13 – 3321Helical; Potential
Transmembrane50 – 7021Helical; Potential
Transmembrane81 – 10121Helical; Potential
Transmembrane110 – 13021Helical; Potential
Transmembrane138 – 15821Helical; Potential
Transmembrane180 – 20021Helical; Potential
Transmembrane201 – 22121Helical; Potential
Transmembrane247 – 26721Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
O31752 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: E364690D8EC9DFC3

FASTA26930,211
        10         20         30         40         50         60 
MVDMKQRILT GVLAAIVFLF LVIVGKLPFT ILIYAMGSVA LFELLRMKKL KLVSLPGLIG 

        70         80         90        100        110        120 
LLLLWMFLLP SQYSFFEADG ISKMEIALFA VLLLLTYTVL VKNTFTFDEV GFITLAAIYI 

       130        140        150        160        170        180 
GMCFHYFIEI RNLDQYGLTY IFYACVVIWS TDSGAYFVGK SLGKRKLWPE ISPNKTVEGF 

       190        200        210        220        230        240 
AGGIVIALVL ATIFQLVAQL PIPYIYLLLI TLFLSVFGQL GDLVESALKR HYDVKDSGNI 

       250        260 
LPGHGGILDR FDSFLFVMPF LYFLLALFS

« Hide

References

[1]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL009126 Genomic DNA. Translation: CAB13527.1.
PIRG69597.
RefSeqNP_389536.1. NC_000964.3.

3D structure databases

ProteinModelPortalO31752.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000000065; EBBACP00000000065; EBBACG00000000065.
GeneID939607.
GenomeReviewsGene locus BSU16540 in contig AL009126_GR.
KEGGbsu:BSU16540.
NMPDRfig|224308.1.peg.1657.
PATRIC18975115. VBIBacSub10457_1749.

Organism-specific databases

GenoListBSU16540. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000000669.
HOGENOMHBG732679.
OMANTFTFDE.
PhylomeDBO31752.
ProtClustDBCLSK887312.

Enzyme and pathway databases

BioCycBSUB:BSU16540-MONOMER.

Family and domain databases

InterProIPR000374. PC_trans.
[Graphical view]
KOK00981.
PfamPF01148. CTP_transf_1. 1 hit.
[Graphical view]
PROSITEPS01315. CDS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCDSA_BACSU
AccessionPrimary (citable) accession number: O31752
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: January 25, 2012
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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