UniProtKB - P46322 (PGSA_BACSU)
Protein
CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
Gene
pgsA
Organism
Bacillus subtilis (strain 168)
Status
Functioni
This protein catalyzes the committed step to the synthesis of the acidic phospholipids.By similarity
Catalytic activityi
- a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycero-3-phospho-(1ʼ-sn-glycero-3ʼ-phosphate) + CMP + H+EC:2.7.8.5
: phosphatidylglycerol biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes phosphatidylglycerol from CDP-diacylglycerol.Proteins known to be involved in the 2 steps of the subpathway in this organism are:
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (pgsA), CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (pgsA)
- no protein annotated in this organism
View all proteins of this organism that are known to be involved in the subpathway that synthesizes phosphatidylglycerol from CDP-diacylglycerol, the pathway phosphatidylglycerol biosynthesis and in Phospholipid metabolism.
GO - Molecular functioni
- CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity Source: UniProtKB-EC
GO - Biological processi
- glycerophospholipid biosynthetic process Source: GO_Central
- phosphatidylglycerol biosynthetic process Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Transferase |
Biological process | Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism |
Enzyme and pathway databases
BioCyci | BSUB:BSU16920-MONOMER |
UniPathwayi | UPA00084;UER00503 |
Names & Taxonomyi
Protein namesi | Recommended name: CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC:2.7.8.5)Alternative name(s): Phosphatidylglycerophosphate synthase Short name: PGP synthase |
Gene namesi | Name:pgsA Synonyms:ymfN Ordered Locus Names:BSU16920 |
Organismi | Bacillus subtilis (strain 168) |
Taxonomic identifieri | 224308 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Proteomesi |
|
Subcellular locationi
- Cell membrane Curated; Multi-pass membrane protein Curated Note: Localized in the septal membrane. The septal localization depends on FtsZ.1 Publication
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transmembranei | 8 – 28 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 39 – 59 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 88 – 108 | HelicalSequence analysisAdd BLAST | 21 | |
Transmembranei | 157 – 177 | HelicalSequence analysisAdd BLAST | 21 |
GO - Cellular componenti
- integral component of membrane Source: UniProtKB-KW
- plasma membrane Source: UniProtKB-SubCell
Keywords - Cellular componenti
Cell membrane, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000056772 | 1 – 193 | CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferaseAdd BLAST | 193 |
Proteomic databases
PaxDbi | P46322 |
PRIDEi | P46322 |
Family & Domainsi
Sequence similaritiesi
Belongs to the CDP-alcohol phosphatidyltransferase class-I family.Curated
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | COG0558, Bacteria |
InParanoidi | P46322 |
OMAi | PIADKAI |
PhylomeDBi | P46322 |
Family and domain databases
Gene3Di | 1.20.120.1760, 1 hit |
InterProi | View protein in InterPro IPR000462, CDP-OH_P_trans IPR043130, CDP-OH_PTrfase_TM_dom IPR004570, Phosphatidylglycerol_P_synth |
Pfami | View protein in Pfam PF01066, CDP-OH_P_transf, 1 hit |
PIRSFi | PIRSF000847, Phos_ph_gly_syn, 1 hit |
TIGRFAMsi | TIGR00560, pgsA, 1 hit |
PROSITEi | View protein in PROSITE PS00379, CDP_ALCOHOL_P_TRANSF, 1 hit |
i Sequence
Sequence statusi: Complete.
P46322-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MFNLPNKITL ARIALIPIFM IIMLAPFDWG RLEVGDESIP VAHLAGAILF
60 70 80 90 100
IIASTTDWVD GYYARKLNLV TNFGKFLDPL ADKLLVSAAL IILVQFDLAP
110 120 130 140 150
AWMVIVIISR EFAVTGLRLV LAGTGEVVAA NMLGKIKTWA QIIAVSALLL
160 170 180 190
HNLPFELVSF PFADLALWVA VFFTVVSGWE YFSKNWEALK TSN
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D50064 Genomic DNA Translation: BAA46041.1 U87792 Genomic DNA Translation: AAB47707.1 AL009126 Genomic DNA Translation: CAB13565.2 |
PIRi | E69675 |
RefSeqi | NP_389574.2, NC_000964.3 WP_003244753.1, NZ_JNCM01000035.1 |
Genome annotation databases
EnsemblBacteriai | CAB13565; CAB13565; BSU16920 |
GeneIDi | 51991302 939675 |
KEGGi | bsu:BSU16920 |
PATRICi | fig|224308.179.peg.1833 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D50064 Genomic DNA Translation: BAA46041.1 U87792 Genomic DNA Translation: AAB47707.1 AL009126 Genomic DNA Translation: CAB13565.2 |
PIRi | E69675 |
RefSeqi | NP_389574.2, NC_000964.3 WP_003244753.1, NZ_JNCM01000035.1 |
3D structure databases
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Protein-protein interaction databases
STRINGi | 224308.BSU16920 |
Proteomic databases
PaxDbi | P46322 |
PRIDEi | P46322 |
Genome annotation databases
EnsemblBacteriai | CAB13565; CAB13565; BSU16920 |
GeneIDi | 51991302 939675 |
KEGGi | bsu:BSU16920 |
PATRICi | fig|224308.179.peg.1833 |
Phylogenomic databases
eggNOGi | COG0558, Bacteria |
InParanoidi | P46322 |
OMAi | PIADKAI |
PhylomeDBi | P46322 |
Enzyme and pathway databases
UniPathwayi | UPA00084;UER00503 |
BioCyci | BSUB:BSU16920-MONOMER |
Family and domain databases
Gene3Di | 1.20.120.1760, 1 hit |
InterProi | View protein in InterPro IPR000462, CDP-OH_P_trans IPR043130, CDP-OH_PTrfase_TM_dom IPR004570, Phosphatidylglycerol_P_synth |
Pfami | View protein in Pfam PF01066, CDP-OH_P_transf, 1 hit |
PIRSFi | PIRSF000847, Phos_ph_gly_syn, 1 hit |
TIGRFAMsi | TIGR00560, pgsA, 1 hit |
PROSITEi | View protein in PROSITE PS00379, CDP_ALCOHOL_P_TRANSF, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PGSA_BACSU | |
Accessioni | P46322Primary (citable) accession number: P46322 Secondary accession number(s): O31772, Q79B77 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1995 |
Last sequence update: | June 16, 2009 | |
Last modified: | December 2, 2020 | |
This is version 124 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families