P0ABG3 (CDSA_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	SF0165, S0168

Organism

Shigella flexneri [Complete proteome] [HAMAP]

Taxonomic identifier

623 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length	285 AA.
Sequence status	Complete.
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 inner membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the CDS family.
Sequence caution	The sequence AAN41827.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAP15708.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	CDP-diacylglycerol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 285	285	Phosphatidate cytidylyltransferase		PRO_0000090746
Regions
	Transmembrane	10 – 30	21	Helical; Potential
	Transmembrane	56 – 76	21	Helical; Potential
	Transmembrane	93 – 113	21	Helical; Potential
	Transmembrane	121 – 141	21	Helical; Potential
	Transmembrane	151 – 171	21	Helical; Potential
	Transmembrane	190 – 210	21	Helical; Potential
	Transmembrane	213 – 233	21	Helical; Potential
	Transmembrane	264 – 284	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	P0ABG3 [UniParc]. Last modified November 13, 2007. Version 2. Checksum: 0D77DCD5EC5FBA9F	FASTA	285	31,454
	10 20 30 40 50 60 MLKYRLISAF VLIPVVIAAL FLLPPVGFAI VTLVVCMLAA WEWGQLSGFT TRSQRVWLAV 70 80 90 100 110 120 LCGLLLALML FLLPEYHRNI HQPLVEISLW ASLGWWIVAL LLVLFYPGSA AIWRNSKTLR 130 140 150 160 170 180 LIFGVLTIVP FFWGMLALRA WHYDENHYSG AIWLLYVMIL VWGADSGAYM FGKLFGKHKL 190 200 210 220 230 240 APKVSPGKTW QGFIGGLATA AVISWGYGMW ANLDVAPVTL LICSIVAALA SVLGDLTESM 250 260 270 280 FKREAGIKDS GHLIPGHGGI LDRIDSLTAA VPVFACLLLL VFRTL

References

[1]

"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157." Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J. Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 301 / Serotype 2a.

[2]

"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T." Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R. Infect. Immun. 71:2775-2786(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005674 Genomic DNA. Translation: AAN41827.2. Different initiation. AE014073 Genomic DNA. Translation: AAP15708.1. Different initiation.
RefSeq	NP_706120.4. NC_004337.2. NP_835903.2. NC_004741.1.
3D structure databases
ProteinModelPortal	P0ABG3.
ModBase	Search...
Protein-protein interaction databases
STRING	198214.SF0165.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAN41827; AAN41827; SF0165. AAP15708; AAP15708; S0168.
GeneID	1024478. 1076599.
KEGG	sfl:SF0165. sfx:S0168.
PATRIC	18701288. VBIShiFle31049_0185.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0575.
HOGENOM	HOG000006168.
KO	K00981.
OMA	WEWGRLN.
ProtClustDB	PRK11624.
Enzyme and pathway databases
UniPathway	UPA00557; UER00614.
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_SHIFL

Accession

Primary (citable) accession number: P0ABG3
Secondary accession number(s): P06466

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	November 13, 2007
Last modified:	May 1, 2013
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program