Summary: Stage II sporulation protein E (SpoIIE)
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Stage II sporulation protein E (SpoIIE) Provide feedback
This family contains a number of bacterial stage II sporulation E proteins ( EC:184.108.40.206). These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments .
Barak I, Behari J, Olmedo G, Guzman P, Brown DP, Castro E, Walker D, Westpheling J, Youngman P; , Mol Microbiol 1996;19:1047-1060.: Structure and function of the Bacillus SpoIIE protein and its localization to sites of sporulation septum assembly. PUBMED:8830262 EPMC:8830262
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This tab holds annotation information from the InterPro database.
InterPro entry IPR001932
This domain is found in protein phosphatase 2C, as well as other proteins eg. pyruvate dehydrogenase (lipoamide)-phosphatase (EC), adenylate cyclase (EC) and some bacterial stage II sporulation E proteins (EC).
Protein phosphatase 2C (PP2C) is one of the four major classes of mammalian serine/threonine specific protein phosphatases (EC). PP2C [PUBMED:1312947] is a monomeric enzyme of about 42 Kd which shows broad substrate specificity and is dependent on divalent cations (mainly manganese and magnesium) for its activity. Its exact physiological role is still unclear. Three isozymes are currently known in mammals: PP2C-alpha, -beta and -gamma. In yeast, there are at least four PP2C homologs: phosphatase PTC1 [PUBMED:8395005], which has weak tyrosine phosphatase activity in addition to its activity on serines, phosphatases PTC2 and PTC3, and hypothetical protein YBR125c. Isozymes of PP2C are also known from Arabidopsis thaliana (ABI1, PPH1), Caenorhabditis elegans (FEM-2, F42G9.1, T23F11.1), Leishmania chagasi and Paramecium tetraurelia. In A. thaliana, the kinase associated protein phosphatase (KAPP) [PUBMED:7973632] is an enzyme that dephosphorylates the Ser/Thr receptor-like kinase RLK5 and which contains a C-terminal PP2C domain.
PP2C does not seem to be evolutionary related to the main family of serine/ threonine phosphatases: PP1, PP2A and PP2B. However, it is significantly similar to the catalytic subunit of pyruvate dehydrogenase phosphatase EC (PDPC) [PUBMED:8396421], which catalyzes dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex. PDPC is a mitochondrial enzyme and, like PP2C, is magnesium-dependent.
|Molecular function||catalytic activity (GO:0003824)|
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Curation and family details
|Seed source:||Pfam-B_17063 (release 10.0)|
|Author:||Vella Briffa B|
|Number in seed:||173|
|Number in full:||6344|
|Average length of the domain:||192.30 aa|
|Average identity of full alignment:||20 %|
|Average coverage of the sequence by the domain:||35.38 %|
|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:||7|
|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 SpoIIE domain has been found. There are 23 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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