| Accession |
MF_01398 |
| Dates |
9-MAR-2009 (Created) 30-JUN-2011 (Last updated, Version 12) |
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
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 (By similarity).
FUNCTION: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0) (By similarity).
case <OG:Chloroplast> or <Property:PHOTOSYN> and not <OC:Chlorobi> and not <OC:Chloroflexi>
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 (By similarity).
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 (By similarity).
end case
case <OG:Chloroplast>
SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein (By similarity).
else case <OC:Cyanobacteria> and not <OC:Gloeobacter>
SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein (By similarity).
else case <OC:Gloeobacter>
SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein (By similarity).
else case not defined <Property:Membrane> or <Property:Membrane=1>
SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein (By similarity).
else case <Property:Membrane=2>
SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein (By similarity).
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.
| Pfam |
PF00430; ATP-synt_B; 1;
|
| TIGRFAMs |
TIGR01144; ATP_synt_b; 1;
|
| General |
Transmembrane; -; 1; trigger=Yes;
|
case <OG:Chloroplast> or <OC:Cyanobacteria> and not <OC:Gloeobacter>
else case <OC:Gloeobacter>
else case not defined <Property:Membrane> or <Property:Membrane=1>
else case <Property:Membrane=2>
end case
GO:0046933; Molecular function: hydrogen ion transporting ATP synthase activity, rotational mechanism.
case <OC:Cyanobacteria> and not <OC:Gloeobacter>
GO:0042651; Cellular component: thylakoid membrane.
else case <OG:Chloroplast>
GO:0009535; Cellular component: chloroplast thylakoid membrane.
else
GO:0042777; Biological process: plasma membrane ATP synthesis coupled proton transport.
GO:0005886; Cellular component: plasma membrane.
end case
| Size range: |
143-326 amino acids |
| Related UniRules: |
MF_01399 (ATPX) |
| Template: |
P0ABA0 (ATPF_ECOLI); P09221 (ATPF_BACP3); Q0ZS23 (ATPF_CLOPD); Q2RFX5 (ATPF_MOOTA); O05333 (ATPF_RHOCA): [Recover all] |
| Scope: |
Bacteria
Plastid |
| Fusion: |
Nter: None; Cter: MF_01416 (atpD) |
| Duplicate: |
in ACAM1, ACICJ, NOSS1, ANTSP, BARHE, BARQU, BART1, BEII9, BIFLO, BRUA1, BRUA2, BRUC2, BRUO2, BRUSI, BRUSU, CYAA5, DESOH, DINSH, GLUOX, GRABC, MARMM, MARMS, MESSB, METCA, MYCA1, MYCA9, MYCBO, MYCBP, MYCGI, MYCLB, MYCLE, MYCMM, MYCPA, MYCS2, MYCSJ, MYCSK, MYCSS, MYCTA, MYCTU, MYCUA, MYCVP, NITMU, OCHA4, OCHNE, PARL1, PELCD, PELLD, PELPD, PROA2, PSEA6, PSEAE, RALSO, RHILO, RHOBA, RHOCS, RHOFD, STRPN, SYNAS, SYNP1, SYNP2, SYNP6, SYNY3, VIBHB, VIBSP, XANP2 |
| Plasmid encoded: |
in ACAM1, SYNP2 |
| Comments: |
Quite a few non-model bacteria have more than 1 copy of this protein, including 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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