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10  structures 2088  species 0  interactions 4233  sequences 22  architectures

Family: BolA (PF01722)

Summary: BolA-like protein

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

This is the Wikipedia entry entitled "BolA-like protein family". More...

BolA-like protein family Edit Wikipedia article

BolA
PDB 1ny8 EBI.jpg
solution structure of protein yrba from escherichia coli: northeast structural genomics consortium target er115
Identifiers
Symbol BolA
Pfam PF01722
InterPro IPR002634
SCOP 1v9j
SUPERFAMILY 1v9j

In molecular biology, the BolA-like protein family consists of the morpho-protein BolA from Escherichia coli and its various homologs. 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.[1] The expression of BolA is growth rate regulated and is induced during the transition into the stationary phase.[1] BolA is also induced by stress during early stages of growth [1] 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.[1][2]

References[edit]

  1. ^ a b c d 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. PMID 10361282. 
  2. ^ 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 402084. PMID 2684651. 

This article incorporates text from the public domain Pfam and InterPro IPR002634

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

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 [1]. The expression of BolA is growth rate regulated and is induced during the transition into the the stationary phase [1]. BolA is also induced by stress during early stages of growth [1] 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].

Literature references

  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

  2. 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


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002634

This family consist of the morpho-protein BolA from Escherichia coli and its various homologs. 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].

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(238)
Full
(4233)
Representative proteomes NCBI
(2705)
Meta
(2605)
RP15
(378)
RP35
(743)
RP55
(1064)
RP75
(1342)
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Format an alignment

  Seed
(238)
Full
(4233)
Representative proteomes NCBI
(2705)
Meta
(2605)
RP15
(378)
RP35
(743)
RP55
(1064)
RP75
(1342)
Alignment:
Format:
Order:
Sequence:
Gaps:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(238)
Full
(4233)
Representative proteomes NCBI
(2705)
Meta
(2605)
RP15
(378)
RP35
(743)
RP55
(1064)
RP75
(1342)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_1996 (release 4.1)
Previous IDs: none
Type: Family
Author: Bashton M, Bateman A
Number in seed: 238
Number in full: 4233
Average length of the domain: 73.30 aa
Average identity of full alignment: 33 %
Average coverage of the sequence by the domain: 73.74 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.7 25.7
Trusted cut-off 25.7 25.8
Noise cut-off 25.6 25.3
Model length: 76
Family (HMM) version: 13
Download: download the raw HMM for this family

Species distribution

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Structures

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 10 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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