UniProtKB - P44570 (PGPB_HAEIN)
Protein
Phosphatidylglycerophosphatase B
Gene
pgpB
Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Functioni
Catalyzes the dephosphorylation of diacylglycerol diphosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG). Also has undecaprenyl pyrophosphate phosphatase activity, required for the biosynthesis of the lipid carrier undecaprenyl phosphate. Can also use lysophosphatidic acid (LPA) and phosphatidylglycerophosphate as substrates. The pattern of activities varies according to subcellular location, PGP phosphatase activity is higher in the cytoplasmic membrane, whereas PA and LPA phosphatase activities are higher in the outer membrane. Activity is independent of a divalent cation ion and insensitive to inhibition by N-ethylmaleimide (By similarity).By similarity
Catalytic activityi
- 1,2-diacyl-sn-glycero-3-phospho-(1ʼ-sn-glycero-3ʼ-phosphate) + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphateEC:3.1.3.27
- EC:3.1.3.81
- EC:3.1.3.4
- di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H+ + phosphateEC:3.6.1.27
: phosphatidylglycerol biosynthesis Pathwayi
This protein is involved in step 2 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)
- Phosphatidylglycerophosphatase B (pgpB), Phosphatidylglycerophosphatase A (pgpA)
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.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 160 | Proton donor; for a subset of substratesBy similarity | 1 | |
Active sitei | 209 | NucleophileBy similarity | 1 | |
Sitei | 213 | Stabilizes the active site histidine for nucleophilic attackBy similarity | 1 |
GO - Molecular functioni
- diacylglycerol diphosphate phosphatase activity Source: UniProtKB-EC
- phosphatidate phosphatase activity Source: UniProtKB-EC
- phosphatidylglycerophosphatase activity Source: UniProtKB-EC
- undecaprenyl-diphosphatase activity Source: UniProtKB-EC
GO - Biological processi
- phosphatidylglycerol biosynthetic process Source: UniProtKB-UniPathway
- phospholipid catabolic process Source: UniProtKB-KW
Keywordsi
Molecular function | Hydrolase |
Biological process | Lipid degradation, Lipid metabolism, Phospholipid degradation, Phospholipid metabolism |
Enzyme and pathway databases
BioCyci | HINF71421:G1GJ1-221-MONOMER |
UniPathwayi | UPA00084;UER00504 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:pgpB Ordered Locus Names:HI_0211 |
Organismi | Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) |
Taxonomic identifieri | 71421 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › |
Proteomesi |
|
Subcellular locationi
Plasma membrane
- Cell inner membrane By similarity; Multi-pass membrane protein By similarity
Other locations
- Cell outer membrane By similarity; Multi-pass membrane protein By similarity
Plasma Membrane
- plasma membrane Source: GO_Central
Other locations
- cell outer membrane Source: UniProtKB-SubCell
- integral component of membrane Source: UniProtKB-KW
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transmembranei | 1 – 21 | HelicalBy similarityAdd BLAST | 21 | |
Topological domaini | 22 – 52 | PeriplasmicBy similarityAdd BLAST | 31 | |
Transmembranei | 53 – 62 | HelicalBy similarity | 10 | |
Topological domaini | 63 – 67 | CytoplasmicBy similarity | 5 | |
Transmembranei | 68 – 91 | HelicalBy similarityAdd BLAST | 24 | |
Topological domaini | 92 – 158 | PeriplasmicBy similarityAdd BLAST | 67 | |
Transmembranei | 159 – 173 | HelicalBy similarityAdd BLAST | 15 | |
Topological domaini | 174 – 184 | CytoplasmicBy similarityAdd BLAST | 11 | |
Transmembranei | 185 – 204 | HelicalBy similarityAdd BLAST | 20 | |
Topological domaini | 205 – 210 | PeriplasmicBy similarity | 6 | |
Transmembranei | 211 – 235 | HelicalBy similarityAdd BLAST | 25 | |
Topological domaini | 236 – 241 | CytoplasmicBy similarity | 6 |
Keywords - Cellular componenti
Cell inner membrane, Cell membrane, Cell outer membrane, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000058363 | 1 – 241 | Phosphatidylglycerophosphatase BAdd BLAST | 241 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 94 – 102 | Phosphatase sequence motif ICurated | 9 | |
Regioni | 157 – 160 | Phosphatase sequence motif IICurated | 4 | |
Regioni | 202 – 213 | Phosphatase sequence motif IIICuratedAdd BLAST | 12 |
Sequence similaritiesi
Belongs to the PA-phosphatase related phosphoesterase family.Curated
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | COG0671, Bacteria |
HOGENOMi | CLU_083863_0_0_6 |
OMAi | AWFLWCL |
PhylomeDBi | P44570 |
Family and domain databases
InterProi | View protein in InterPro IPR036938, P_Acid_Pase_2/haloperoxi_sf IPR000326, P_Acid_Pase_2/haloperoxidase |
Pfami | View protein in Pfam PF01569, PAP2, 1 hit |
SMARTi | View protein in SMART SM00014, acidPPc, 1 hit |
SUPFAMi | SSF48317, SSF48317, 1 hit |
i Sequence
Sequence statusi: Complete.
P44570-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MFKRLSLYTL LLCLVPFFIW GISYQWHGNS QLTQADYWLY LLTETGSVPY
60 70 80 90 100
ALITCVLFTL LFAFLFKNPK QWILGVIVMG ISVIATQAAK TGAKALFEEP
110 120 130 140 150
RPFTVYLAEQ THSTPENFYK NDRTLRAEIA KNFYSMDAIT PAWLVHHYEN
160 170 180 190 200
ETGYSFPSGH TIFAATWLML AVGFTQLLGN RSFKAKLLVV GIAVWGLLML
210 220 230 240
ISRVRLGMHY PIDLLVATLL AWLINSIIFA FLKKKAIFVM K
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L42023 Genomic DNA Translation: AAC21879.1 |
PIRi | I64054 |
RefSeqi | NP_438379.1, NC_000907.1 WP_005694086.1, NC_000907.1 |
Genome annotation databases
EnsemblBacteriai | AAC21879; AAC21879; HI_0211 |
KEGGi | hin:HI_0211 |
PATRICi | fig|71421.8.peg.215 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L42023 Genomic DNA Translation: AAC21879.1 |
PIRi | I64054 |
RefSeqi | NP_438379.1, NC_000907.1 WP_005694086.1, NC_000907.1 |
3D structure databases
SMRi | P44570 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 71421.HI_0211 |
Genome annotation databases
EnsemblBacteriai | AAC21879; AAC21879; HI_0211 |
KEGGi | hin:HI_0211 |
PATRICi | fig|71421.8.peg.215 |
Phylogenomic databases
eggNOGi | COG0671, Bacteria |
HOGENOMi | CLU_083863_0_0_6 |
OMAi | AWFLWCL |
PhylomeDBi | P44570 |
Enzyme and pathway databases
UniPathwayi | UPA00084;UER00504 |
BioCyci | HINF71421:G1GJ1-221-MONOMER |
Family and domain databases
InterProi | View protein in InterPro IPR036938, P_Acid_Pase_2/haloperoxi_sf IPR000326, P_Acid_Pase_2/haloperoxidase |
Pfami | View protein in Pfam PF01569, PAP2, 1 hit |
SMARTi | View protein in SMART SM00014, acidPPc, 1 hit |
SUPFAMi | SSF48317, SSF48317, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PGPB_HAEIN | |
Accessioni | P44570Primary (citable) accession number: P44570 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1995 |
Last sequence update: | November 1, 1995 | |
Last modified: | April 7, 2021 | |
This is version 114 of the entry and version 1 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