Reviewed, UniProtKB/Swiss-Prot Q92JJ2 (PGSA_RICCN)

Names and origin

Protein names

Recommended name:
    CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
    EC=2.7.8.5
Alternative name(s):
    Phosphatidylglycerophosphate synthase
      Short name=PGP synthase

Gene names

Name:	pgsA
Ordered Locus Names:	RC0075

Organism

Rickettsia conorii [Complete proteome] [HAMAP]

Taxonomic identifier

781 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › spotted fever group

Protein attributes

Sequence length	181 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	This protein catalyzes the committed step to the synthesis of the acidic phospholipids By similarity.
Catalytic activity	CDP-diacylglycerol + sn-glycerol 3-phosphate = CMP + 3(3-sn-phosphatidyl)-sn-glycerol 1-phosphate.
Pathway	Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Subcellular location	Cell membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the CDP-alcohol phosphatidyltransferase class-I family.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Cell membrane Membrane
Domain	Transmembrane
Molecular function	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	CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase 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 – 181	181	CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase		PRO_0000056782
Regions
	Transmembrane	8 – 28	21	Potential
	Transmembrane	35 – 55	21	Potential
	Transmembrane	64 – 84	21	Potential
	Transmembrane	148 – 168	21	Potential

Sequences

	Sequence		Length	Mass (Da)
	Q92JJ2-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 31539AA0F39E40F0	FASTA	181	20,328
	10 20 30 40 50 60 MRIDKNLPNY LTIARIMVIP VIILVFYINN SLARTLGALL FVLASITDFF DGYIARKYNL 70 80 90 100 110 120 VTSFGKMFDP IADKLLVGCV IIMLLKKDNV DEIPCLLILA REFLVSGLRE FLALVKVSVP 130 140 150 160 170 180 VSRLAKVKTF LQMFALSILI LGSKGSGIIY LDIVGEIILW IAAFLTIITG YSYFKACKKY F

References

[1]

"Mechanisms of evolution in Rickettsia conorii and R. prowazekii." Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D. Science 293:2093-2098(2001) [PubMed: 11557893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE006914 Genomic DNA. Translation: AAL02613.1.
PIR	C97709.
RefSeq	NP_359712.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	928586.
GenomeReviews	Gene locus RC0075 in contig AE006914_GR.
KEGG	rco:RC0075.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q92JJ2.
OMA	TSNIGRM.
Enzyme and pathway databases
BioCyc	RCON272944:RC0075-MON.
BRENDA	2.7.8.5. 267518.
Family and domain databases
InterPro	IPR000462. CDP-OH_P_trans. IPR004570. Phosphatidylglycerol_P_synth. [Graphical view]
Pfam	PF01066. CDP-OH_P_transf. 1 hit. [Graphical view]
PIRSF	PIRSF000847. Phos_ph_gly_syn. 1 hit.
TIGRFAMs	TIGR00560. pgsA. 1 hit.
PROSITE	PS00379. CDP_ALCOHOL_P_TRANSF. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PGSA_RICCN

Accession

Primary (citable) accession number: Q92JJ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 26, 2002
Last sequence update:	December 1, 2001
Last modified:	November 3, 2009
This is version 51 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)