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HAMAP rule MF_01398

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General rule information [?]

Accession MF_01398
Dates 9-MAR-2009 (Created)
17-FEB-2023 (Last updated, Version 33)
Name ATP_synth_b_bprime
Scope
Bacteria
Plastid
Templates P0ABA0 (ATPF_ECOLI); P09221 (ATPF_BACP3); Q0ZS23 (ATPF_CLOPD); Q2RFX5 (ATPF_MOOTA); O05333 (ATPF_RHOCA): [Recover all]
case <OC:Bacteria> or <OG:Chloroplast>
Triggered by
end case


Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
ATPF
case <OC:Bacteria>
Protein name
RecName: Full=ATP synthase subunit b;
AltName: Full=ATP synthase F(0) sector subunit b;
AltName: Full=ATPase subunit I;
AltName: Full=F-type ATPase subunit b;
Short=F-ATPase subunit b;
else case <OG:Chloroplast>
Protein name
RecName: Full=ATP synthase subunit b, chloroplastic;
AltName: Full=ATP synthase F(0) sector subunit b;
AltName: Full=ATPase subunit I;
end case
Gene name
atpF

Comments [?]

Function F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
case <OG:Chloroplast> or <OC:Cyanobacteriota>
Subunit F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains.
else
Subunit F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains.
end case
case <OG:Chloroplast>
Subcellular location Plastid, chloroplast thylakoid membrane; Single-pass membrane protein.
else case <OC:Cyanobacteriota> and not <OC:Gloeobacter>
Subcellular location Cellular thylakoid membrane; Single-pass membrane protein.
else case <OC:Gloeobacter>
Subcellular location Cell inner membrane; Single-pass membrane protein.
else case not defined <Property:Membrane> or <Property:Membrane=1>
Subcellular location Cell membrane; Single-pass membrane protein.
else case <Property:Membrane=2>
Subcellular location Cell inner membrane; Single-pass membrane protein.
end case
case <OG:Chloroplast>
Miscellaneous In plastids the F-type ATPase is also known as CF(1)CF(0).
end case
Similarity Belongs to the ATPase B chain family.

Keywords [?]

ATP synthesis
CF(0)
Hydrogen ion transport
Ion transport
Membrane
Transmembrane
Transport
case <OG:Chloroplast> or <OC:Cyanobacteriota> and not <OC:Gloeobacter>
Thylakoid
else case <OC:Gloeobacter>
Cell membrane
Cell inner membrane
else case not defined <Property:Membrane> or <Property:Membrane=1>
Cell membrane
else case <Property:Membrane=2>
Cell membrane
Cell inner membrane
end case
Transmembrane helix

Gene Ontology [?]

GO:0046933; Molecular function: proton-transporting ATP synthase activity, rotational mechanism.
GO:0015986; Biological process: proton motive force-driven ATP synthesis.
case <OC:Cyanobacteriota> and not <OC:Gloeobacter>
GO:0042651; Cellular component: thylakoid membrane.
else case <OG:Chloroplast>
GO:0009535; Cellular component: chloroplast thylakoid membrane.
else
GO:0005886; Cellular component: plasma membrane.
end case

Cross-references [?]

Pfam PF00430; ATP-synt_B; 1;
TIGRFAMs TIGR01144; ATP_synt_b; 1;

Computed features [?]

General Transmembrane; -; 1; trigger=yes;

Additional information [?]

Size range 143-326 amino acids
Related rules MF_01399 (ATPF2 supersedes the current rule)
Fusion Nter: None; Cter: MF_01416 (atpD)
Comments MF_01398 signature matches b and b' subunits, but this rule is specific for b subunit annotation. See MF_01399 for b' subunit annotation. This family includes potential copies of the b' subunit in non- cyanobacteria; however all are now called subunit b. Quite a few non-model bacteria have more than 1 copy of this protein, including potential copies of the b' subunit; exactly which copies are found in the enzyme requires more study. In Mycoplasma pneumoniae (ATCC 29342 / M129) this is a lipoprotein; this is suggested for similar Mycoplasmataceae. Sometimes predicted to have 2 transmembrane helices. In some of the Mycobacteria one copy is fused with the delta subunit. Some have a longer C-terminus. For a review on the peripheral (stator) stalk see PubMed=16730323; DOI=10.1016/j.bbabio.2006.04.007; Weber J.; "ATP synthase: subunit-subunit interactions in the stator stalk."; Biochim. Biophys. Acta 1757:1162-1170(2006).


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