P0ABF8 (PGSA_ECOLI) 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:	b1912, JW1897

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	182 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from direct assay Ref.1. Source: EcoliWiki plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity Inferred from direct assay Ref.1. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Probable
	Chain	2 – 182	181	CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase HAMAP MF_01437		PRO_0000056773
Regions
	Topological domain	2 – 13	12	Cytoplasmic Potential
	Transmembrane	14 – 38	25	Helical; Potential
	Topological domain	39 – 61	23	Periplasmic Potential
	Transmembrane	62 – 82	21	Helical; Potential
	Topological domain	83 – 87	5	Cytoplasmic Potential
	Transmembrane	88 – 108	21	Helical; Potential
	Topological domain	109 – 146	38	Periplasmic Potential
	Transmembrane	147 – 169	23	Helical; Potential
	Topological domain	170 – 182	13	Cytoplasmic Potential
Experimental info
	Mutagenesis	60	1	T → P in pgsA3; lower activity.
	Mutagenesis	92	1	T → I in pgsA10; lower activity.

Sequences

	Sequence		Length	Mass (Da)
	P0ABF8 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: F8F0502ABE6DC8D5	FASTA	182	20,701
	10 20 30 40 50 60 MQFNIPTLLT LFRVILIPFF VLVFYLPVTW SPFAAALIFC VAAVTDWFDG FLARRWNQST 70 80 90 100 110 120 RFGAFLDPVA DKVLVAIAMV LVTEHYHSWW VTLPAATMIA REIIISALRE WMAELGKRSS 130 140 150 160 170 180 VAVSWIGKVK TTAQMVALAW LLWRPNIWVE YAGIALFFVA AVLTLWSMLQ YLSAARADLL DQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and expression of the gene locus encoding the phosphatidylglycerophosphate synthase of Escherichia coli." Gopalakrishnan A.S., Chen Y.-C., Temkin M., Dowhan W. J. Biol. Chem. 261:1329-1338(1986) [PubMed: 3003065] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Primary structures of the wild-type and mutant alleles encoding the phosphatidylglycerophosphate synthase of Escherichia coli." Usui M., Sembongi H., Matsuzaki H., Matsumoto K., Shibuya I. J. Bacteriol. 176:3389-3392(1994) [PubMed: 8195097] [Abstract] Cited for: SEQUENCE REVISION, MUTANTS PGSA3 AND PGSA10. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:379-392(1996) [PubMed: 9097040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Phosphatidylglycerophosphate synthase from Escherichia coli." Dowhan W. Methods Enzymol. 209:313-321(1992) [PubMed: 1323047] [Abstract] Cited for: REVIEW.
[7]	"Global topology analysis of the Escherichia coli inner membrane proteome." Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G. Science 308:1321-1323(2005) [PubMed: 15919996] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: K12 / MG1655 / ATCC 47076.
[8]	"Two-dimensional 1H-NMR of transmembrane peptides from Escherichia coli phosphatidylglycerophosphate synthase in micelles." Morein S., Trouard T.P., Hauksson J.B., Arvidson G., Lindblom G. Eur. J. Biochem. 241:489-497(1996) [PubMed: 8917447] [Abstract] Cited for: STRUCTURE BY NMR OF 6-25 AND 149-176.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M12299 Genomic DNA. Translation: AAA98754.1. U00096 Genomic DNA. Translation: AAC74979.1. AP009048 Genomic DNA. Translation: BAA15732.1.
PIR	XNECPG. E64954.
RefSeq	NP_416422.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P0ABF8.
ModBase	Search...
Protein-protein interaction databases
IntAct	P0ABF8. 1 interaction.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000001160; EBESCP00000001160; EBESCG00000000956. EBESCT00000016484; EBESCP00000015775; EBESCG00000015544.
GeneID	945791.
GenomeReviews	Gene locus JW1897 in contig AP009048_GR. Gene locus b1912 in contig U00096_GR.
KEGG	ecj:JW1897. eco:b1912.
PATRIC	32119157. VBIEscCol129921_1993.
Organism-specific databases
EchoBASE	EB0700.
EcoGene	EG10706. pgsA.
Phylogenomic databases
eggNOG	COG0558.
GeneTree	EBGT00050000009502.
HOGENOM	HBG686655.
OMA	WSYMAAS.
PhylomeDB	P0ABF8.
ProtClustDB	PRK10832.
Enzyme and pathway databases
BioCyc	EcoCyc:PHOSPHAGLYPSYN-MONOMER. MetaCyc:PHOSPHAGLYPSYN-MONOMER.
Gene expression databases
Genevestigator	P0ABF8.
Family and domain databases
HAMAP	MF_01437. PgsA. [Tree]
InterPro	IPR000462. CDP-OH_P_trans. IPR023762. PGP_synthase_bac. IPR004570. Phosphatidylglycerol_P_synth. [Graphical view]
KO	K00995.
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_ECOLI

Accession

Primary (citable) accession number: P0ABF8
Secondary accession number(s): P06978

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program