Summary: Rare lipoprotein A (RlpA)-like double-psi beta-barrel
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Rare lipoprotein A (RlpA)-like double-psi beta-barrel Provide feedback
Rare lipoprotein A (RlpA) contains a conserved region that has the double-psi beta-barrel (DPBB) fold [3,4]. The function of RlpA is not well understood, but it has been shown to act as a prc mutant suppressor in Escherichia coli . The DPBB fold is often an enzymatic domain. The members of this family are quite diverse, and if catalytic this family may contain several different functions. Another example of this domain is found in the N terminus of pollen allergen.
Bass S, Gu Q, Christen A; , J Bacteriol 1996;178:1154-1161.: Multicopy suppressors of prc mutant Escherichia coli include two HtrA (DegP) protease homologs (HhoAB), DksA, and a truncated R1pA. PUBMED:8576052 EPMC:8576052
Takase I, Ishino F, Wachi M, Kamata H, Doi M, Asoh S, Matsuzawa H, Ohta T, Matsuhashi M; , J Bacteriol 1987;169:5692-5699.: Genes encoding two lipoproteins in the leuS-dacA region of the Escherichia coli chromosome. PUBMED:3316191 EPMC:3316191
Mizuguchi K, Dhanaraj V, Blundell TL, Murzin AG; , Structure Fold Des. 1999;7:215-216.: N-ethylmaleimide-sensitive fusion protein (NSF) and CDC48 confirmed as members of the double-psi beta-barrel aspartate decarboxylase/formate dehydrogenase family. PUBMED:10610264 EPMC:10610264
Castillo RM, Mizuguchi K, Dhanaraj V, Albert A, Blundell TL, Murzin AG; , Structure Fold Des 1999;7:227-236.: A six-stranded double-psi beta barrel is shared by several protein superfamilies. PUBMED:10368289 EPMC:10368289
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR009009
Beta barrels are commonly observed in protein structures. They are classified in terms of two integral parameters: the number of strands in the sheet, n, and the shear number, S, a measure of the stagger of the strands in the beta-sheet. These two parameters have been shown to determine the major geometrical features of beta-barrels. Six-stranded beta-barrels with a pseudo-twofold axis are found in several proteins. One involving parallel strands forming two psi structures is known as the double-psi barrel. The first psi structure consists of the loop connecting strands beta1 and beta2 (a 'psi loop') and the strand beta5, whereas the second psi structure consists of the loop connecting strands beta4 and beta5 and the strand beta2. All the psi structures in double-psi barrels have a unique handedness, in that beta1 (beta4), beta2 (beta5) and the loop following beta5 (beta2) form a right-handed helix. The unique handedness may be related to the fact that the twisting angle between the parallel pair of strands is always larger than that between the antiparallel pair [PUBMED:10368289].
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The DPBB fold is often an enzymatic domain. The members of this family are quite diverse, and if catalytic this family may contain several different functions [1,2]. This clan represents the barwin like barrels.
The clan contains the following 5 members:3D Barwin Cerato-platanin DPBB_1 Glyco_hydro_45
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_3255 (release 6.5)|
|Author:||Mifsud W, Studholme DJ|
|Number in seed:||127|
|Number in full:||5162|
|Average length of the domain:||87.00 aa|
|Average identity of full alignment:||26 %|
|Average coverage of the sequence by the domain:||33.33 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the DPBB_1 domain has been found. There are 5 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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