HAMAP rule MF_01398
General rule information
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| Accession | MF_01398 |
| Dates | 9-MAR-2009 (Created)
7-DEC-2023 (Last updated, Version 36) |
| Name | ATP_synth_b_bprime |
| Scope(s) |
Bacteria Plastid |
| Template(s) | P0ABA0 (ATPF_ECOLI); P09221 (ATPF_BACP3); Q0ZS23 (ATPF_CLOPD); Q2RFX5 (ATPF_MOOTA); O05333 (ATPF_RHOCA); [ Recover all ] |
| Triggered by |
case c? <OC:Bacteria> or <OG:Chloroplast>
HAMAP; MF_01398 (Get profile general information and statistics) end case
|
Propagated annotation
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Identifier, protein and gene names
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| 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 | Name=atpF; |
Comments
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| 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. |
| FUNCTION | 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
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| 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
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| GO:0046933; Molecular function:proton-transporting ATP synthase activity, rotational mechanism | |
| GO:0015986; Biological process:proton motive force-driven ATP synthesis | |
| case <OCellular component:Cyanobacteriota> and not <OC:Gloeobacter> | |
| GO:0042651; Cellular component:thylakoid membrane | |
| else case <OG:Chloroplast> | |
| GO:0009535; Cellular component:chloroplast thylakoid membrane | |
| else; https://www.ebi.ac.uk/QuickGO/term/else | |
| GO:0005886; Cellular component:plasma membrane | |
| end case | |
Cross-references
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| Pfam | PF00430; ATP-synt_B; 1; |
| NCBIfam | TIGR01144; ATP_synt_b; 1; |
| General | Transmembrane; -; 1; |
Features
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Additional information
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| Size range | 143-326 amino acids |
| Related rules |
MF_01399 |
| 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). |