PPGR - Gene Detail

Basic Information

Gene ID	Bpev01.c5492.g0005 View in Genome Browser
Position	Contig5492:4848-5461 (-) 613bp
Gene Type	gene
Gene Description (Protein Product)	Belongs to the ABC transporter superfamily
Organism	Betula pendula
Also AS

upstream:

Domain

Database	EntryID	E-Value	Start	end	InterPro ID	Description

Regulation&Interaction

Protein-protein interaction (PPI)

Bpev01.c5567.g0001 Phage-related protein, tail component

Bpev01.c5636.g0002 Folding helper with both chaperone and peptidyl-prolyl cis-trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa-Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction. SlyD could be involved in Tat-dependent translocation, by binding to the Tat-type signal of folded proteins

Bpev01.c5501.g0001 pts system

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Annotation

Orthologous Group

Orthologous ID	Species Number	All hits in PereRegDB	Hits of this species	Orthologous Detail

Expression Profile

DataSet	Number of Samples expressed(TPM>1)	Mean	Min	Max	Standard deviation(SD)	Coeffcient variation(CV)

Select Expression

Pathway

GO Term	Description	GO Category
GO:0000166	nucleotide binding	MF
GO:0003674	molecular_function	MF
GO:0005488	binding	MF
GO:0005524	ATP binding	MF
GO:0005575	cellular_component	CC
GO:0005623	obsolete cell	CC
GO:0005886	plasma membrane	CC
GO:0008144	obsolete drug binding	MF
GO:0016020	membrane	CC
GO:0017076	purine nucleotide binding	MF
GO:0030554	adenyl nucleotide binding	MF
GO:0032553	ribonucleotide binding	MF
GO:0032555	purine ribonucleotide binding	MF
GO:0032559	adenyl ribonucleotide binding	MF
GO:0035639	purine ribonucleoside triphosphate binding	MF
GO:0036094	small molecule binding	MF
GO:0043167	ion binding	MF
GO:0043168	anion binding	MF
GO:0044464	obsolete cell part	CC
GO:0071944	cell periphery	CC
GO:0097159	organic cyclic compound binding	MF
GO:0097367	carbohydrate derivative binding	MF
GO:1901265	nucleoside phosphate binding	MF
GO:1901363	heterocyclic compound binding	MF

KEGG Term	Name	Description
map02010	ABC transporters	The ATP-binding cassette (ABC) transporters form one of the largest known protein families, and are widespread in bacteria, archaea, and eukaryotes. They couple ATP hydrolysis to active transport of a wide variety of substrates such as ions, sugars, lipids, sterols, peptides, proteins, and drugs. The structure of a prokaryotic ABC transporter usually consists of three components; typically two integral membrane proteins each having six transmembrane segments, two peripheral proteins that bind and hydrolyze ATP, and a periplasmic (or lipoprotein) substrate-binding protein. Many of the genes for the three components form operons as in fact observed in many bacterial and archaeal genomes. On the other hand, in a typical eukaryotic ABC transporter, the membrane spanning protein and the ATP-binding protein are fused, forming a multi-domain protein with the membrane-spanning domain (MSD) and the nucleotide-binding domain (NBD).
map02010	ABC transporters	The ATP-binding cassette (ABC) transporters form one of the largest known protein families, and are widespread in bacteria, archaea, and eukaryotes. They couple ATP hydrolysis to active transport of a wide variety of substrates such as ions, sugars, lipids, sterols, peptides, proteins, and drugs. The structure of a prokaryotic ABC transporter usually consists of three components; typically two integral membrane proteins each having six transmembrane segments, two peripheral proteins that bind and hydrolyze ATP, and a periplasmic (or lipoprotein) substrate-binding protein. Many of the genes for the three components form operons as in fact observed in many bacterial and archaeal genomes. On the other hand, in a typical eukaryotic ABC transporter, the membrane spanning protein and the ATP-binding protein are fused, forming a multi-domain protein with the membrane-spanning domain (MSD) and the nucleotide-binding domain (NBD).