Summary: Stage II sporulation protein E (SpoIIE)
Stage II sporulation protein E (SpoIIE) Provide feedback
This family contains a number of bacterial stage II sporulation E proteins ( EC:126.96.36.199). 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
This tab holds annotation information from the InterPro database.
InterPro entry IPR001932
Protein phosphatases remove phosphate groups from various proteins that are the key components of a number of signalling pathways in eukaryotes and prokaryotes. Protein phosphatases that dephosphorylate Ser and Thr residues are classified into the phosphoprotein (PPP) and the protein phosphatase Mg(2+)- or Mn(2+)-dependent (PPM) families. The core structure of PPMs is the 300-residue PPM-type phosphatase domain that catalyzes the dephosphorylation of phosphoserine- and phosphothreonine-containing protein. The PPM-type phosphatase domain is found as a module in diverse structural contexts and is modulated by targeting and regulatory subunits [PUBMED:9003755, PUBMED:9869399, PUBMED:22115775, PUBMED:22668558].
Some proteins known to contain a PPM-type phosphatase domain are listed below:
- Bacillus subtilis stage II sporulation protein E (SpoIIE), controls the sporulation by dephosphorylating an anti-transcription factor SpoIIAA, reversing the actions of the SpoIIAB protein kinase in a process that is gouverned by the ADP/ATP ratio [levdikov].
- Mycobacterium tuberculosis PP2C-family Ser/Thr phosphatase (PstP).
- Eucaryotic PP2C, a negative regulator of protein kinase cascades that are activated as a result of stress.
- Yeast adenyl cyclase, plays essential roles in regulation of cellular metabolism by catalyzing the synthesis of a second messenger, cAMP.
- Mammalian mitochondrial pyruvate dehydrogenase phosphatase 1 (PDP1).
- Plant kinase-associated protein phosphatase (KAPP), regulates receptor-like kinase (RLK) signalling pathways.
- Plant absissic acid-insenstive 1 and 2 (ABI1 and ABI2), play a key absissic acid (ABA) signal transduction.
The PP2C-type phosphatase domain consists of 10 segments of beta-strands and 5 segments of alpha-helix and comprises a pair of detached subdomains. The first is a small beta-sandwich with strand beta1 packed against strands beta2 and beta3; the second is a larger beta-sandwich in which a four-stranded beta- heet packs against a three-stranded beta-sheet with flanking alpha-helices [PUBMED:9003755, PUBMED:22115775].
This entry represents a conserved region found in the N-terminal part that contains a perfectly conserved tripeptide.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||catalytic activity (GO:0003824)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the UniProtKB sequence database using the family HMM
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
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Curation and family details
|Seed source:||Pfam-B_17063 (release 10.0)|
|Author:||Vella Briffa B|
|Number in seed:||156|
|Number in full:||4481|
|Average length of the domain:||195.20 aa|
|Average identity of full alignment:||19 %|
|Average coverage of the sequence by the domain:||35.55 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||9|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 33 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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