Summary: BolA-like protein
This is the Wikipedia entry entitled "BolA-like protein family". More...
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BolA-like protein family Edit Wikipedia article
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solution structure of protein yrba from escherichia coli: northeast structural genomics consortium target er115
In molecular biology, the BolA-like protein family consists of the morpho-protein BolA from Escherichia coli, the Fra2 protein from Saccharomyces cerevisiae, and various homologs. The BolA protein is a DNA-binding regulator; the Fra2 protein is an iron sulfur cluster protein that binds Grx3/4 and is involved in regulating iron levels .
In E. coli, over-expression of this protein causes round morphology and may be involved in switching the cell between elongation and septation systems during cell division. The expression of BolA is growth rate regulated and is induced during the transition into the stationary phase. BolA is also induced by stress during early stages of growth  and may have a general role in stress response. It has also been suggested that BolA can induce the transcription of penicillin binding proteins 6 and 5.
- Dressaire C, Moreira RN, Barahona S, Alves de Matos AP, Arraiano CM, Santos JM, Freire P, Vicente M, Arraiano CM (17 February 2015). "BolA Is a Transcriptional Switch That Turns Off Motility and Turns On Biofilm Development". mBio. 6 (1): e02352–14. doi:10.1128/mBio.02352-14. PMC . PMID 25691594.
- Li H, Mapolelo DT, Dingra NN, Naik SG, Lees NS, Hoffman BM, Riggs-Gelasco PJ, Huynh BH, Johnson MK, Outten CE (2009). "The yeast iron regulatory proteins Grx3/4 and Fra2 form heterodimeric complexes containing a [2Fe-2S] cluster with cysteinyl and histidyl ligation". Biochemistry. 48 (40): 9569–81. doi:10.1021/bi901182w. PMC . PMID 19715344.
- Santos JM, Freire P, Vicente M, Arraiano CM (May 1999). "The stationary-phase morphogene bolA from Escherichia coli is induced by stress during early stages of growth". Mol. Microbiol. 32 (4): 789–98. doi:10.1046/j.1365-2958.1999.01397.x. PMID 10361282.
- Aldea M, Garrido T, Hernandez-Chico C, Vicente M, Kushner SR (December 1989). "Induction of a growth-phase-dependent promoter triggers transcription of bolA, an Escherichia coli morphogene". EMBO J. 8 (12): 3923–31. PMC . PMID 2684651.
BolA-like protein Provide feedback
This family consist of the morphoprotein BolA from E. coli and its various homologues. In E. coli over expression of this protein causes round morphology and may be involved in switching the cell between elongation and septation systems during cell division . The expression of BolA is growth rate regulated and is induced during the transition into the the stationary phase . BolA is also induced by stress during early stages of growth  and may have a general role in stress response. It has also been suggested that BolA can induce the transcription of penicillin binding proteins 6 and 5 [2,1].
Santos JM, Freire P, Vicente M, Arraiano CM; , Mol Microbiol 1999;32:789-798.: The stationary-phase morphogene bolA from Escherichia coli is induced by stress during early stages of growth. PUBMED:10361282 EPMC:10361282
Aldea M, Garrido T, Hernandez-Chico C, Vicente M, Kushner SR; , EMBO J 1989;8:3923-3931.: Induction of a growth-phase-dependent promoter triggers transcription of bolA, an Escherichia coli morphogene. PUBMED:2684651 EPMC:2684651
Internal database links
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002634This family consist of the morpho-protein BolA from Escherichia coli and its various homologues. In E. coli, over-expression of this protein causes round morphology and may be involved in switching the cell between elongation and septation systems during cell division [PUBMED:10361282]. The expression of BolA is growth rate regulated and is induced during the transition into the the stationary phase [PUBMED:10361282]. BolA is also induced by stress during early stages of growth [PUBMED:10361282] and may have a general role in stress response. It has also been suggested that BolA can induce the transcription of penicillin binding proteins 6 and 5 [PUBMED:2684651, PUBMED:10361282]. IbaG is a BolA homologue involved in acid resistance [PUBMED:22534295].
- 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_1996 (release 4.1)|
|Author:||Bashton M, Bateman A|
|Number in seed:||411|
|Number in full:||4625|
|Average length of the domain:||72.60 aa|
|Average identity of full alignment:||30 %|
|Average coverage of the sequence by the domain:||66.69 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||17|
|Download:||download the raw HMM for this family|
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There is 1 interaction 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 BolA 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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