Reviewed, UniProtKB/Swiss-Prot O31752 (CDSA_BACSU)

Names and origin

Protein names

Recommended 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:	BSU16540

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	269 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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 process	Phospholipid biosynthesis
Cellular component	Cell membrane Membrane
Domain	Transmembrane
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	phosphatidate cytidylyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 269	269	Phosphatidate cytidylyltransferase		PRO_0000090726
Regions
	Transmembrane	13 – 33	21	Potential
	Transmembrane	50 – 70	21	Potential
	Transmembrane	81 – 101	21	Potential
	Transmembrane	110 – 130	21	Potential
	Transmembrane	138 – 158	21	Potential
	Transmembrane	180 – 200	21	Potential
	Transmembrane	201 – 221	21	Potential
	Transmembrane	247 – 267	21	Potential

Sequences

	Sequence		Length	Mass (Da)
	O31752-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: E364690D8EC9DFC3	FASTA	269	30,211
	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

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. , 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
EMBLGenBankDDBJ	AL009126 Genomic DNA. Translation: CAB13527.1.
PIR	G69597.
RefSeq	NP_389536.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	939607.
GenomeReviews	Gene locus BSU16540 in contig AL009126_GR.
KEGG	bsu:BSU16540.
NMPDR	fig|224308.1.peg.1657.
Organism-specific databases
SubtiList	BG12575. cdsA. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	O31752.
OMA	YHIFFIF.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU1655-MON.
BRENDA	2.7.7.41. 150.
Family and domain databases
InterPro	IPR000374. PC_trans. [Graphical view]
Pfam	PF01148. CTP_transf_1. 1 hit. [Graphical view]
PROSITE	PS01315. CDS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CDSA_BACSU

Accession

Primary (citable) accession number: O31752

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	November 3, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)