NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=LT2;
PubMed=2548058 [NCBI, ExPASy, EBI, Israel, Japan]
Garrett A.R., Johnson L.A., Beacham I.R.;
"Isolation, molecular characterization and expression of the ushB gene of Salmonella typhimurium which encodes a membrane-bound UDP-sugar hydrolase.";
Mol. Microbiol. 3:177-186(1989).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LT2 / SGSC1412 / ATCC 700720;
DOI=10.1038/35101614; PubMed=11677609 [NCBI, ExPASy, EBI, Israel, Japan]
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.;
"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
Nature 413:852-856(2001).

Comments

CATALYTIC ACTIVITY: CDP-diacylglycerol + H₂O = CMP + phosphatidate.
PATHWAY: Phospholipid metabolism; CDP-diacylglycerol degradation; phosphatidate from CDP-diacylglycerol: step 1/1 .
SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein.
SIMILARITY: Belongs to the cdh family.
CAUTION: Was originally (PubMed:2548058) thought to be a UDP-sugar hydrolase.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X13380; CAA31757.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE008889; AAL22904.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S04172; S04172.

RefSeq

NP_462945.1; -.

3D structure databases

ModBase

P26219.

Enzyme and pathway databases

BioCyc

STYP99287:STM4064-MON; -.

Organism-specific databases

StyGene

SG10051; cdh.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from HAMAP).
GO:0008715;	Molecular function: CDP-diacylglycerol diphosphatase activity (inferred from electronic annotation from HAMAP).
GO:0008654;	Biological process: phospholipid biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00319; -; 1.
PBIL [Tree]

InterPro

IPR003763; CDP-diacylglyc_Pase_bac.
IPR015993; CDP-diacylglyc_Pase_proteobac.
Graphical view of domain structure.

Pfam

PF02611; CDH; 1.
Pfam graphical view of domain structure.

PIRSF001273; CDH; 1.

TIGR00672; cdh; 1.

Genome annotation databases

GeneID

1255591; -.

GenomeReviews

AE006468_GR; STM4064.

KEGG

stm:STM4064; -.

Phylogenomic databases

HOGENOM

P26219; -.

Genome annotation databases

CMR

P26219; STM4064.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell inner membrane; Cell membrane; Complete proteome; Hydrolase; Membrane; Phospholipid biosynthesis; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 251`	`251`	`CDP-diacylglycerol pyrophosphatase.`	`PRO_0000198583`
`TRANSMEM`	`5 25`	`21`	`Potential.`
`CONFLICT`	`13 13`		`V -> L (in Ref. 1; CAA31757).`

Sequence information

Length: 251 AA [This is the length of the unprocessed precursor]

Molecular weight: 28368 Da [This is the MW of the unprocessed precursor]

CRC64: 2F4BBAB49BD870BE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKKTGYFLLA VIVIVAAAGV GYWKFSGNPD ALREIVLEQC LPDQLQHQNP APCAEVKPRA 

        70         80         90        100        110        120 
GYVVFKDRHG PLQYLLMPTY RINGTESPLL LEPATPNFFW LAWQARGYMS KKYGHDIPDS 

       130        140        150        160        170        180 
AVSLAINSRL GRSQDHLHIH ISCIRPDVRE QLDNDLTRIS TRWLPLPGGL MGHEYLARRV 

       190        200        210        220        230        240 
TESELAQRSP FMMLAEEVPE ARDHMGRYAL AVVRQSDDSF VLLATERNLL TFNRASAEEI 

       250 
QDHSCAILSS R

P26219 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools