Q66BN4 (PGSA_YERPS) Reviewed, UniProtKB/Swiss-Prot

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:	YPTB1737

Organism

Yersinia pseudotuberculosis serotype I (strain IP32953) [Complete proteome] [HAMAP]

Taxonomic identifier

273123 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia › Yersinia pseudotuberculosis

Protein attributes

Sequence length	182 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	This protein catalyzes the committed step to the synthesis of the acidic phospholipids By similarity. HAMAP-Rule MF_01437
Catalytic activity	CDP-diacylglycerol + sn-glycerol 3-phosphate = CMP + 3(3-sn-phosphatidyl)-sn-glycerol 1-phosphate. HAMAP-Rule MF_01437
Pathway	Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2. HAMAP-Rule MF_01437
Subcellular location	Cell inner membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_01437.
Sequence similarities	Belongs to the CDP-alcohol phosphatidyltransferase class-I family.

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	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	phosphatidylglycerol 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	CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 182	182	CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase HAMAP-Rule MF_01437		PRO_0000239136
Regions
	Topological domain	1 – 12	12	Cytoplasmic Potential
	Transmembrane	13 – 37	25	Helical; Potential
	Topological domain	38 – 60	23	Periplasmic Potential
	Transmembrane	61 – 81	21	Helical; Potential
	Topological domain	82 – 86	5	Cytoplasmic Potential
	Transmembrane	87 – 107	21	Helical; Potential
	Topological domain	108 – 145	38	Periplasmic Potential
	Transmembrane	146 – 168	23	Helical; Potential
	Topological domain	169 – 181	13	Cytoplasmic Potential

Sequences

	Sequence		Length	Mass (Da)
	Q66BN4 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 5227A0724C651B9D	FASTA	182	20,806
	10 20 30 40 50 60 MQLNIPTWLT LFRVVLIPFF VLAFYLPFVW APMVCAIIFV FAAATDWFDG FLARRWKQTT 70 80 90 100 110 120 RFGAFLDPVA DKVMVAVALV LVAEHYHSWW ITLPAATMIA REIIISSLRE WMAEIGKRSS 130 140 150 160 170 180 VAVSWVGKVK TMAQMGSLVG LLWRPDHNVE LASFVLLYIA AVLTFWSMFQ YLNAAWSDLL EP

References

[1]

"Insights into the evolution of Yersinia pestis through whole-genome comparison with Yersinia pseudotuberculosis." Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., Simonet M., Chenal-Francisque V., Souza B. , Dacheux D., Elliott J.M., Derbise A., Hauser L.J., Garcia E. Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: IP32953.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX936398 Genomic DNA. Translation: CAH20976.1.
RefSeq	YP_070263.1. NC_006155.1.
3D structure databases
ProteinModelPortal	Q66BN4.
ModBase	Search...
Protein-protein interaction databases
STRING	273123.YPTB1737.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAH20976; CAH20976; YPTB1737.
GeneID	2956246.
KEGG	yps:YPTB1737.
PATRIC	18642183. VBIYerPse22266_2155.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0558.
HOGENOM	HOG000010898.
KO	K00995.
OMA	WSYMAAS.
ProtClustDB	PRK10832.
Enzyme and pathway databases
UniPathway	UPA00084; UER00503.
Family and domain databases
HAMAP	MF_01437. PgsA.
InterPro	IPR000462. CDP-OH_P_trans. IPR023762. PGP_synthase_bac. 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_YERPS

Accession

Primary (citable) accession number: Q66BN4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program