Summary: Cell surface heme-binding protein Shp
Cell surface heme-binding protein Shp Provide feedback
Shp is part of a complex which functions in heme uptake in Streptococcus pyogenes. During which, Shp transfers its heme to HtsA which is a component of an ABC transporter. The heme binding region of Shp contains an immunoglobulin-like beta-sandwich fold and has a unique heme-iron coordination with the axial ligands being two methionine residues from the same Shp molecule . Surrounding the heme pocket, there is a negative surface which may serve as a docking interface for heme transfer .
Aranda R 4th, Worley CE, Liu M, Bitto E, Cates MS, Olson JS, Lei B, Phillips GN Jr; , J Mol Biol. 2007;374:374-383.: Bis-methionyl coordination in the crystal structure of the heme-binding domain of the streptococcal cell surface protein Shp. PUBMED:17920629 EPMC:17920629
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This tab holds annotation information from the InterPro database.
InterPro entry IPR020985
Shp is a cell-surface protein which forms part of a complex responsible for haem uptake in Streptococcus pyogenes. During haem uptake Shp transfers a bound haem to HtsA, the lipoprotein component of an ABC transporter. This entry represents the haem-binding domain of Shp. It contains an immunoglobulin-like beta-sandwich fold and has a unique haem-iron coordination, with the axial ligands being two methionine residues from the same Shp molecule [PUBMED:17920629]. Surrounding the haem pocket, there is a negative surface which may serve as a docking interface for haem transfer.
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Curation and family details
|Number in seed:||3|
|Number in full:||63|
|Average length of the domain:||148.50 aa|
|Average identity of full alignment:||42 %|
|Average coverage of the sequence by the domain:||44.61 %|
|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|
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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 HemeBinding_Shp domain has been found. There are 2 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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