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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.

Pathway:iphosphatidylglycerol 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)
  2. Phosphatidylglycerophosphatase C (pgpC), Phosphatidylglycerophosphatase B (pgpB)
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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000002673 Componenti: Chromosome UP000001006 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88CytoplasmicBy similarity
Transmembranei9 – 2921HelicalSequence AnalysisAdd
BLAST
Topological domaini30 – 4718PeriplasmicBy similarityAdd
BLAST
Transmembranei48 – 6821HelicalSequence AnalysisAdd
BLAST
Topological domaini69 – 713CytoplasmicBy similarity
Transmembranei72 – 9221HelicalSequence AnalysisAdd
BLAST
Topological domaini93 – 15866PeriplasmicBy similarityAdd
BLAST
Transmembranei159 – 17921HelicalSequence AnalysisAdd
BLAST
Topological domaini180 – 1845CytoplasmicBy similarity
Transmembranei185 – 20521HelicalSequence AnalysisAdd
BLAST
Topological domaini206 – 2105PeriplasmicBy similarity
Transmembranei211 – 23121HelicalSequence AnalysisAdd
BLAST
Topological domaini232 – 25423CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 254254Phosphatidylglycerophosphatase BPRO_0000058364Add
BLAST

Post-translational modificationi

The N-terminus is blocked.By similarity

Interactioni

Protein-protein interaction databases

STRINGi198214.SF1282.

Structurei

3D structure databases

ProteinModelPortaliP0A926.
SMRiP0A926. Positions 2-254.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 1059Phosphatase sequence motif I
Regioni160 – 1634Phosphatase sequence motif II
Regioni200 – 21112Phosphatase sequence motif IIIAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0671.
HOGENOMiHOG000286191.
KOiK01096.
OMAiYALITCV.
OrthoDBiEOG60CWKV.

Family and domain databases

Gene3Di1.20.144.10. 2 hits.
InterProiIPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamiPF01569. PAP2. 1 hit.
[Graphical view]
SMARTiSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMiSSF48317. SSF48317. 2 hits.

Sequencei

Sequence statusi: Complete.

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_LM651928.1.

Genome annotation databases

EnsemblBacteriaiAAN42894; AAN42894; SF1282.
AAP16778; AAP16778; S1365.
GeneIDi1024235.
KEGGisfl:SF1282.
PATRICi18703976. VBIShiFle31049_1492.

Cross-referencesi

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_LM651928.1.

3D structure databases

ProteinModelPortaliP0A926.
SMRiP0A926. Positions 2-254.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198214.SF1282.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN42894; AAN42894; SF1282.
AAP16778; AAP16778; S1365.
GeneIDi1024235.
KEGGisfl:SF1282.
PATRICi18703976. VBIShiFle31049_1492.

Phylogenomic databases

eggNOGiCOG0671.
HOGENOMiHOG000286191.
KOiK01096.
OMAiYALITCV.
OrthoDBiEOG60CWKV.

Enzyme and pathway databases

UniPathwayiUPA00084; UER00504.

Family and domain databases

Gene3Di1.20.144.10. 2 hits.
InterProiIPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamiPF01569. PAP2. 1 hit.
[Graphical view]
SMARTiSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMiSSF48317. SSF48317. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
    Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
    , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
    Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 301 / Serotype 2a.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700930 / 2457T / Serotype 2a.

Entry informationi

Entry nameiPGPB_SHIFL
AccessioniPrimary (citable) accession number: P0A926
Secondary accession number(s): P18201
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: July 22, 2015
This is version 72 of the entry and version 1 of the sequence. [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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.