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5  structures 1312  species 0  interactions 1662  sequences 2  architectures

Family: Potass_KdpF (PF09604)

Summary: F subunit of K+-transporting ATPase (Potass_KdpF)

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F subunit of K+-transporting ATPase (Potass_KdpF) Provide feedback

This entry describes a very small integral membrane peptide KdpF, a subunit of the K(+)-translocating Kdp complex. It is found upstream of the KdpA subunit (IPR004623). Because of its very small size and highly hydrophobic character, it is sometimes missed in genome annotation.

This tab holds annotation information from the InterPro database.

InterPro entry IPR011726

Transmembrane ATPases are membrane-bound enzyme complexes/ion transporters that use ATP hydrolysis to drive the transport of protons across a membrane. Some transmembrane ATPases also work in reverse, harnessing the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP.

There are several different types of transmembrane ATPases, which can differ in function (ATP hydrolysis and/or synthesis), structure (e.g., F-, V- and A-ATPases, which contain rotary motors) and in the type of ions they transport [ PUBMED:15473999 , PUBMED:15078220 ]. The different types include:

  • F-ATPases (ATP synthases, F1F0-ATPases), which are found in mitochondria, chloroplasts and bacterial plasma membranes where they are the prime producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts).
  • V-ATPases (V1V0-ATPases), which are primarily found in eukaryotes and they function as proton pumps that acidify intracellular compartments and, in some cases, transport protons across the plasma membrane [ PUBMED:20450191 ]. They are also found in bacteria [ PUBMED:9741106 ].
  • A-ATPases (A1A0-ATPases), which are found in Archaea and function like F-ATPases, though with respect to their structure and some inhibitor responses, A-ATPases are more closely related to the V-ATPases [ PUBMED:18937357 , PUBMED:1385979 ].
  • P-ATPases (E1E2-ATPases), which are found in bacteria and in eukaryotic plasma membranes and organelles, and function to transport a variety of different ions across membranes.
  • E-ATPases, which are cell-surface enzymes that hydrolyse a range of NTPs, including extracellular ATP.

This entry represents the F subunit (KdpF) of a P-type K+ translocating ATPase (Kdp) in archaea and bacteria. KdpF is a very small integral membrane peptide. The kdpABC operon of Escherichia coli codes for the high affinity K+ translocating Kdp complex [ PUBMED:9789555 , PUBMED:10608856 ]. KdpF is found upstream of the KdpA subunit ( INTERPRO ). Because of its very small size and highly hydrophobic character, it is sometimes missed in genome annotation.Though KdpF is not essential in vivo [ PUBMED:9789555 ] it is part of the complex and functions as a stabilising element in vitro [ PUBMED:10608856 ].

Gene Ontology

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Domain organisation

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Alignments

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  Seed
(78)
Full
(1662)
Representative proteomes UniProt
(8521)
RP15
(117)
RP35
(654)
RP55
(1712)
RP75
(3532)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

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

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  Seed
(78)
Full
(1662)
Representative proteomes UniProt
(8521)
RP15
(117)
RP35
(654)
RP55
(1712)
RP75
(3532)
Alignment:
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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
(78)
Full
(1662)
Representative proteomes UniProt
(8521)
RP15
(117)
RP35
(654)
RP55
(1712)
RP75
(3532)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download  
Gzipped 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.

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Curation and family details

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Seed source: TIGRFAMs
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: TIGRFAMs, Coggill P
Number in seed: 78
Number in full: 1662
Average length of the domain: 23.90 aa
Average identity of full alignment: 44 %
Average coverage of the sequence by the domain: 68.60 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.2 21.2
Trusted cut-off 21.2 21.2
Noise cut-off 21.0 21.1
Model length: 24
Family (HMM) version: 12
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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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 Potass_KdpF domain has been found. There are 5 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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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
P36937 View 3D Structure Click here
Q2FWH8 View 3D Structure Click here
Q79FT7 View 3D Structure Click here