P46322 (PGSA_BACSU) 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
Synonyms:	ymfN
Ordered Locus Names:	BSU16920

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	193 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.
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 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 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: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 193	193	CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase		PRO_0000056772
Regions
	Transmembrane	8 – 28	21	Helical; Potential
	Transmembrane	39 – 59	21	Helical; Potential
	Transmembrane	88 – 108	21	Helical; Potential
	Transmembrane	157 – 177	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	P46322 [UniParc]. Last modified June 16, 2009. Version 3. Checksum: BA24E8767819D302	FASTA	193	21,338
	10 20 30 40 50 60 MFNLPNKITL ARIALIPIFM IIMLAPFDWG RLEVGDESIP VAHLAGAILF IIASTTDWVD 70 80 90 100 110 120 GYYARKLNLV TNFGKFLDPL ADKLLVSAAL IILVQFDLAP AWMVIVIISR EFAVTGLRLV 130 140 150 160 170 180 LAGTGEVVAA NMLGKIKTWA QIIAVSALLL HNLPFELVSF PFADLALWVA VFFTVVSGWE 190 YFSKNWEALK TSN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Overexpression of phosphatidylglycerophosphate synthase restores protein translocation in a secG deletion mutant of Escherichia coli at low temperature." Kontinen V.P., Tokuda H. FEBS Lett. 364:157-160(1995) [PubMed: 7750561] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[2]	De Rossi E. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: PB1831.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION TO 2; 45-47 AND 62.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D50064 Genomic DNA. Translation: BAA46041.1. U87792 Genomic DNA. Translation: AAB47707.1. AL009126 Genomic DNA. Translation: CAB13565.2.
PIR	E69675.
RefSeq	NP_389574.2. NC_000964.3.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000002351; EBBACP00000002351; EBBACG00000002346.
GeneID	939675.
GenomeReviews	Gene locus BSU16920 in contig AL009126_GR.
KEGG	bsu:BSU16920.
NMPDR	fig|224308.1.peg.1695.
PATRIC	18975191. VBIBacSub10457_1787.
Organism-specific databases
GenoList	BSU16920. [Micado]
Phylogenomic databases
GeneTree	EBGT00050000002310.
HOGENOM	HBG686655.
PhylomeDB	P46322.
ProtClustDB	CLSK887317.
Enzyme and pathway databases
BioCyc	BSUB:BSU16920-MONOMER.
Family and domain databases
InterPro	IPR000462. CDP-OH_P_trans. 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_BACSU

Accession

Primary (citable) accession number: P46322
Secondary accession number(s): O31772, Q79B77

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	June 16, 2009
Last modified:	January 25, 2012
This is version 89 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program