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Protein

Phosphatidylglycerophosphatase B

Gene

pgpB

Organism
Shigella flexneri
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

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

Phosphatidylglycerophosphate + H2O = phosphatidylglycerol + phosphate.
1,2-diacyl-sn-glycerol 3-diphosphate + H2O = 1,2-diacyl-sn-glycerol 3-phosphate + phosphate.
A 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.
Ditrans,octacis-undecaprenyl diphosphate + H2O = ditrans,octacis-undecaprenyl phosphate + phosphate.

Pathwayi: phosphatidylglycerol biosynthesis

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:
  1. CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (pgsA), CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (pgsA), CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (pgsA), CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (pgsA)
  2. Phosphatidylglycerophosphatase A (pgpA), Phosphatidylglycerophosphatase C (pgpC), Phosphatidylglycerophosphatase A (CBW45_02120), Phosphatidylglycerophosphatase B (pgpB), Phosphatidylglycerophosphatase A (CBL21_06380)
This subpathway is part of the pathway phosphatidylglycerol biosynthesis, which is itself part of Phospholipid metabolism.
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 keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei163Proton donor; for a subset of substratesBy similarity1
Active sitei207NucleophileBy similarity1
Sitei211Stabilizes the active site histidine for nucleophilic attackBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processLipid degradation, Lipid metabolism, Phospholipid degradation, Phospholipid metabolism

Enzyme and pathway databases

UniPathwayiUPA00084; UER00504.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylglycerophosphatase B (EC:3.1.3.27)
Alternative name(s):
Diacylglycerol pyrophosphate phosphatase (EC:3.1.3.81)
Short name:
DGPP phosphatase
Phosphatidate phosphatase (EC:3.1.3.4)
Undecaprenyl pyrophosphate phosphatase (EC:3.6.1.27)
Undecaprenyl-diphosphatase
Gene namesi
Name:pgpB
Ordered Locus Names:SF1282, S1365
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
Proteomesi
  • UP000002673 Componenti: Chromosome
  • UP000001006 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei2 – 24HelicalBy similarityAdd BLAST23
Topological domaini25 – 54PeriplasmicBy similarityAdd BLAST30
Transmembranei55 – 66HelicalBy similarityAdd BLAST12
Topological domaini67 – 71CytoplasmicBy similarity5
Transmembranei72 – 94HelicalBy similarityAdd BLAST23
Topological domaini95 – 161PeriplasmicBy similarityAdd BLAST67
Transmembranei162 – 176HelicalBy similarityAdd BLAST15
Topological domaini177 – 182CytoplasmicBy similarity6
Transmembranei183 – 202HelicalBy similarityAdd BLAST20
Topological domaini203 – 208PeriplasmicBy similarity6
Transmembranei209 – 232HelicalBy similarityAdd BLAST24
Topological domaini233 – 254CytoplasmicBy similarityAdd BLAST22

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Cell outer membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000583642 – 254Phosphatidylglycerophosphatase BAdd BLAST253

Post-translational modificationi

The N-terminus is blocked.By similarity

Proteomic databases

PaxDbiP0A926.

Structurei

3D structure databases

ProteinModelPortaliP0A926.
SMRiP0A926.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni97 – 105Phosphatase sequence motif ICurated9
Regioni160 – 163Phosphatase sequence motif IICurated4
Regioni200 – 211Phosphatase sequence motif IIICuratedAdd BLAST12

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105EYK. Bacteria.
COG0671. LUCA.
HOGENOMiHOG000286191.
KOiK01096.
OMAiAWFLWCL.

Family and domain databases

InterProiView protein in InterPro
IPR036938. P_Acid_Pase_2/haloperoxi_sf.
IPR000326. P_Acid_Pase_2/haloperoxidase.
PfamiView protein in Pfam
PF01569. PAP2. 1 hit.
SMARTiView protein in SMART
SM00014. acidPPc. 1 hit.
SUPFAMiSSF48317. SSF48317. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A926-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSIARRTAV GAALLLVMPV AVWISGWRWQ PGEQSWLLKA AFWVTETVTQ
60 70 80 90 100
PWGVITHLIL FGWFLWCLRF RIKAAFVLFA ILAAAILVGQ GVKSWIKDKV
110 120 130 140 150
QEPRPFVIWL EKTHHIPVDE FYTLKRAERG NLVKEQLAEE KNIPQYLRSH
160 170 180 190 200
WQKETGFAFP SGHTMFAASW ALLAVGLLWP RRRTLTIAIL LVWATGVMGS
210 220 230 240 250
RLLLGMHWPR DLVVATLISW ALVAVATWLA QRICGPLTPP AEENREIAQR

EQES
Length:254
Mass (Da):29,021
Last modified:July 19, 2005 - v1
Checksum:i9F4E6E88C34D458C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN42894.1.
AE014073 Genomic DNA. Translation: AAP16778.1.
RefSeqiNP_707187.1. NC_004337.2.
WP_001256538.1. NZ_NMXZ01000012.1.

Genome annotation databases

EnsemblBacteriaiAAN42894; AAN42894; SF1282.
AAP16778; AAP16778; S1365.
GeneIDi1024235.
KEGGisfl:SF1282.
sfx:S1365.
PATRICifig|198214.7.peg.1503.

Similar proteinsi

Entry informationi

Entry nameiPGPB_SHIFL
AccessioniPrimary (citable) accession number: P0A926
Secondary accession number(s): P18201
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: November 22, 2017
This is version 85 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families