Summary: Hydrophobic surface binding protein A
Hydrophobic surface binding protein A Provide feedback
This protein is found in eukaryotes. Proteins in this family are typically between 171 to 275 amino acids in length. Although the HsbA amino acid sequence suggests that HsbA may be hydrophilic, HsbA adsorbed to hydrophobic PBSA (Polybutylene succinate-co-adipate) surfaces in the presence of NaCl or CaCl2. When HsbA was adsorbed on the hydrophobic PBSA surfaces, it promoted PBSA degradation via the CutL1 polyesterase. CutL1 interacts directly with HsbA attached to the hydrophobic QCM electrode surface. These results suggest that when HsbA is adsorbed onto the PBSA surface, it recruits CutL1, and that when CutL1 is accumulated on the PBSA surface, it stimulates PBSA degradation.
Ohtaki S, Maeda H, Takahashi T, Yamagata Y, Hasegawa F, Gomi K, Nakajima T, Abe K;, Appl Environ Microbiol. 2006;72:2407-2413.: Novel hydrophobic surface binding protein, HsbA, produced by Aspergillus oryzae. PUBMED:16597938 EPMC:16597938
Internal database links
|SCOOP:||Dispanin Lipoprotein_6 Orbi_NS3 UPF0184 Med15_fungi COG6|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR021054
Hydrophobic surface binding proteins are typically between 171 to 275 amino acids in length. Although the HsbA amino acid sequence suggests that HsbA may be hydrophilic, HsbA adsorbed to hydrophobic PBSA (Polybutylene succinate-co-adipate) surfaces in the presence of NaCl or CaCl2. When HsbA was adsorbed on the hydrophobic PBSA surfaces, it promoted PBSA degradation via the CutL1 polyesterase. CutL1 interacts directly with HsbA attached to the hydrophobic QCM electrode surface. These results suggest that when HsbA is adsorbed onto the PBSA surface, it recruits CutL1, and that when CutL1 is accumulated on the PBSA surface, it stimulates PBSA degradation [PUBMED:16597938].
This entry is also characterised by a antigenic cell wall galactomannoprotein in Aspergillus fumigatus, which is a protein of 284 amino acid residues. It contains a serine- and threonine-rich region for O glycosylation, a signal peptide, and a putative glycosylphosphatidyl inositol attachment signal sequence. Ultrastructural analysis showed that the protein is present in the cell walls of hyphae and conidia [PUBMED:11682494].
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This example describes an architecture with one
Gladomain, followed by two consecutive
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We make a range of alignments for each Pfam-A family:
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- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
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- alignment generated by searching the metagenomics sequence database using the family HMM
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Curation and family details
|Seed source:||PFAM-B_3635 (release 23.0)|
|Author:||Assefa S, Gavin OL|
|Number in seed:||71|
|Number in full:||311|
|Average length of the domain:||119.30 aa|
|Average identity of full alignment:||19 %|
|Average coverage of the sequence by the domain:||53.41 %|
|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:||3|
|Download:||download the raw HMM for this family|
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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 HsbA domain has been found. There are 1 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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