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12  structures 4687  species 1  interaction 4809  sequences 2  architectures

Family: ZapA (PF05164)

Summary: Cell division protein ZapA

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This is the Wikipedia entry entitled "ZapA family". More...

ZapA family Edit Wikipedia article

ZapA
PDB 1w2e EBI.jpg
The crystal structure of the bacterial cell division protein ZapA
Identifiers
Symbol ZapA
Pfam PF05164
InterPro IPR007838
SCOP 1t3u
SUPERFAMILY 1t3u

In molecular biology, the ZapA protein family is a group of related proteins that includes the cell division protein ZapA. The structure of ZapA has a core structure consisting of two layers alpha/beta, and has a long C-terminal helix that forms dimeric parallel and tetrameric antiparallel coiled coils.[1] ZapA interacts with FtsZ, where FtsZ is part of a mid-cell cytokinetic structure termed the Z-ring that recruits a hierarchy of fission related proteins early in the bacterial cell cycle. ZapA drives the polymerisation and filament bundling of FtsZ, thereby contributing to the spatio-temporal tuning of the Z-ring.

References

  1. ^ Low HH, Moncrieffe MC, Löwe J (August 2004). "The crystal structure of ZapA and its modulation of FtsZ polymerisation". J. Mol. Biol. 341 (3): 839–52. doi:10.1016/j.jmb.2004.05.031. PMID 15288790. 

This article incorporates text from the public domain Pfam and InterPro IPR007838

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.

Cell division protein ZapA Provide feedback

ZapA is a cell division protein which interacts with FtsZ. FtsZ is part of a mid-cell cytokinetic structure termed the Z-ring that recruits a hierarchy of fission related proteins early in the bacterial cell cycle. The interaction of FtsZ with ZapA drives its polymerisation and promotes FtsZ filament bundling thereby contributing to the spatio-temporal tuning of the Z-ring [1].

Literature references

  1. Low HH, Moncrieffe MC, Lowe J; , J Mol Biol 2004;341:839-852.: The crystal structure of ZapA and its modulation of FtsZ polymerisation. PUBMED:15288790 EPMC:15288790

  2. Gueiros-Filho FJ, Losick R; , Genes Dev 2002;16:2544-2556.: A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ. PUBMED:12368265 EPMC:12368265


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR007838

This entry represents a structural domain found in the cell division protein ZapA, as well as in related proteins. This domain has a core structure consisting of two layers alpha/beta, and has a long C-terminal helix that forms dimeric parallel and tetrameric antiparallel coiled coils [PUBMED:15288790]. ZapA interacts with FtsZ, where FtsZ is part of a mid-cell cytokinetic structure termed the Z-ring that recruits a hierarchy of fission related proteins early in the bacterial cell cycle. ZapA drives the polymerisation and filament bundling of FtsZ, thereby contributing to the spatio-temporal tuning of the Z-ring.

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 (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, 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
(437)
Full
(4809)
Representative proteomes UniProt
(14378)
NCBI
(12497)
Meta
(1381)
RP15
(1199)
RP35
(3224)
RP55
(4930)
RP75
(7226)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(437)
Full
(4809)
Representative proteomes UniProt
(14378)
NCBI
(12497)
Meta
(1381)
RP15
(1199)
RP35
(3224)
RP55
(4930)
RP75
(7226)
Alignment:
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Sequence:
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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
(437)
Full
(4809)
Representative proteomes UniProt
(14378)
NCBI
(12497)
Meta
(1381)
RP15
(1199)
RP35
(3224)
RP55
(4930)
RP75
(7226)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   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.

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: COG3027
Previous IDs: DUF710;
Type: Family
Sequence Ontology: SO:0100021
Author: Finn RD , Mistry J
Number in seed: 437
Number in full: 4809
Average length of the domain: 97.20 aa
Average identity of full alignment: 19 %
Average coverage of the sequence by the domain: 83.35 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.9 20.9
Trusted cut-off 21.0 21.1
Noise cut-off 20.8 20.8
Model length: 88
Family (HMM) version: 13
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

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Interactions

There is 1 interaction for this family. More...

ZapA

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 ZapA domain has been found. There are 12 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 sequence.

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