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3  structures 4775  species 0  interactions 5963  sequences 9  architectures

Family: ATP-synt_B (PF00430)

Summary: ATP synthase B/B' CF(0)

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This is the Wikipedia entry entitled "ATP5F1". More...

ATP5F1 Edit Wikipedia article

ATP synthase, H+ transporting, mitochondrial Fo complex, subunit B1
Identifiers
Symbols ATP5F1; PIG47
External IDs OMIM603270 MGI1100495 HomoloGene1275 GeneCards: ATP5F1 Gene
RNA expression pattern
PBB GE ATP5F1 211755 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 515 11950
Ensembl ENSG00000116459 ENSMUSG00000000563
UniProt P24539 Q9CQQ7
RefSeq (mRNA) NM_001688 NM_009725
RefSeq (protein) NP_001679 NP_033855
Location (UCSC) Chr 1:
111.99 – 112.01 Mb
Chr 3:
105.94 – 105.96 Mb
PubMed search [1] [2]
ATP-synt_B
PDB 1l2p EBI.jpg
atp synthase b subunit dimerization domain
Identifiers
Symbol ATP-synt_B
Pfam PF00430
Pfam clan CL0255
InterPro IPR002146
SCOP 1b9u
SUPERFAMILY 1b9u

ATP synthase subunit b, mitochondrial is an enzyme that in humans is encoded by the ATP5F1 gene.[1][2]

This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the b subunit of the proton channel.[2]

The b subunits are part of the peripheral stalk that links the F1 and FO complexes together, and which acts as a stator to prevent certain subunits from rotating with the central rotary element. The peripheral stalk differs in subunit composition between mitochondrial, chloroplast and bacterial F-ATPases. In bacterial and chloroplast F-ATPases, the peripheral stalk is composed of one copy of the delta subunit (homologous to OSCP in mitochondria), and two copies of subunit b in bacteria, or one copy each of subunits b and b' in chloroplasts and photosynthetic bacteria.[3]

References[edit]

  1. ^ Higuti T, Tsurumi C, Osaka F, Kawamura Y, Tsujita H, Yoshihara Y, Tani I, Tanaka K, Ichihara A (Sep 1991). "Molecular cloning of cDNA for the import precursor of human subunit B of H(+)-ATP synthase in mitochondria". Biochem Biophys Res Commun 178 (3): 1014–20. doi:10.1016/0006-291X(91)90993-H. PMID 1831354. 
  2. ^ a b "Entrez Gene: ATP5F1 ATP synthase, H+ transporting, mitochondrial F0 complex, subunit B1". 
  3. ^ Carbajo RJ, Kellas FA, Runswick MJ, Montgomery MG, Walker JE, Neuhaus D (August 2005). "Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit". J. Mol. Biol. 351 (4): 824–38. doi:10.1016/j.jmb.2005.06.012. PMID 16045926. 

Further reading[edit]


This article incorporates text from the public domain Pfam and InterPro IPR002146

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.

ATP synthase B/B' CF(0) Provide feedback

Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in PF00006

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002146

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 (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 eukaryotic vacuoles and catalyse ATP hydrolysis to transport solutes and lower pH in organelles.
  • 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).
  • 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.

F-ATPases (also known as F1F0-ATPase, or H(+)-transporting two-sector ATPase) (EC) are composed of two linked complexes: the F1 ATPase complex is the catalytic core and is composed of 5 subunits (alpha, beta, gamma, delta, epsilon), while the F0 ATPase complex is the membrane-embedded proton channel that is composed of at least 3 subunits (A-C), nine in mitochondria (A-G, F6, F8). Both the F1 and F0 complexes are rotary motors that are coupled back-to-back. In the F1 complex, the central gamma subunit forms the rotor inside the cylinder made of the alpha(3)beta(3) subunits, while in the F0 complex, the ring-shaped C subunits forms the rotor. The two rotors rotate in opposite directions, but the F0 rotor is usually stronger, using the force from the proton gradient to push the F1 rotor in reverse in order to drive ATP synthesis [PUBMED:11309608]. These ATPases can also work in reverse to hydrolyse ATP to create a proton gradient.

This entry represents subunits B and B' from the F0 complex in F-ATPases found in chloroplasts and in bacterial plasma membranes. The B subunits are part of the peripheral stalk that links the F1 and F0 complexes together, and which acts as a stator to prevent certain subunits from rotating with the central rotary element. The peripheral stalk differs in subunit composition between mitochondrial, chloroplast and bacterial F-ATPases. In bacterial and chloroplast F-ATPases, the peripheral stalk is composed of one copy of the delta subunit (homologous to OSCP in mitochondria), and two copies of subunit B in bacteria, or one copy each of subunits B and B' in chloroplasts and photosynthetic bacteria [PUBMED:16045926].

More information about this protein can be found at Protein of the Month: ATP Synthases [PUBMED:].

Gene Ontology

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Domain organisation

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

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Pfam Clan

This family is a member of clan ATP_synthase (CL0255), which contains the following 12 members:

ATP-synt_8 ATP-synt_B FliH Fun_ATP-synt_8 HrpE Mt_ATP-synt_B NolV OSCP V-ATPase_G vATP-synt_E Yae1_N YMF19

Alignments

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  Seed
(27)
Full
(5963)
Representative proteomes NCBI
(3817)
Meta
(3365)
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(418)
RP35
(853)
RP55
(1083)
RP75
(1260)
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  Seed
(27)
Full
(5963)
Representative proteomes NCBI
(3817)
Meta
(3365)
RP15
(418)
RP35
(853)
RP55
(1083)
RP75
(1260)
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
(27)
Full
(5963)
Representative proteomes NCBI
(3817)
Meta
(3365)
RP15
(418)
RP35
(853)
RP55
(1083)
RP75
(1260)
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

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Pfam alignments:

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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: Pfam-B_137 (release 1.0)
Previous IDs: none
Type: Family
Author: Finn RD
Number in seed: 27
Number in full: 5963
Average length of the domain: 130.10 aa
Average identity of full alignment: 24 %
Average coverage of the sequence by the domain: 75.06 %

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 24.5 24.5
Trusted cut-off 24.5 24.6
Noise cut-off 24.4 24.4
Model length: 132
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 ATP-synt_B domain has been found. There are 3 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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