AC   MF_01398;
DC   Protein; auto
c?   <OC:Bacteria> or <OG:Chloroplast>
TR   HAMAP; MF_01398; -; 1; level=0
XX
Names: ATP_synth_b_bprime
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ID   ATPF
case <OC:Bacteria>
DE   RecName: Full=ATP synthase subunit b;
DE   AltName: Full=ATP synthase F(0) sector subunit b;
DE   AltName: Full=ATPase subunit I;
DE   AltName: Full=F-type ATPase subunit b;
DE            Short=F-ATPase subunit b;
else case <OG:Chloroplast>
DE   RecName: Full=ATP synthase subunit b, chloroplastic;
DE   AltName: Full=ATP synthase F(0) sector subunit b;
DE   AltName: Full=ATPase subunit I;
end case
GN   Name=atpF;
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CC   -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC       of a proton or sodium gradient. F-type ATPases consist of two
CC       structural domains, F(1) containing the extramembraneous catalytic core
CC       and F(0) containing the membrane proton channel, linked together by a
CC       central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC       in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC       the central stalk subunits to proton translocation.
CC   -!- FUNCTION: Component of the F(0) channel, it forms part of the
CC       peripheral stalk, linking F(1) to F(0).
case <OG:Chloroplast> or <OC:Cyanobacteriota>
CC   -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC       - and F(0) - the membrane proton channel. F(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main
CC       subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains
CC       form an alternating ring which encloses part of the gamma chain. F(1)
CC       is attached to F(0) by a central stalk formed by the gamma and epsilon
CC       chains, while a peripheral stalk is formed by the delta, b and b'
CC       chains.
else
CC   -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC       - and F(0) - the membrane proton channel. F(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main
CC       subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an
CC       alternating ring which encloses part of the gamma chain. F(1) is
CC       attached to F(0) by a central stalk formed by the gamma and epsilon
CC       chains, while a peripheral stalk is formed by the delta and b chains.
end case
case <OG:Chloroplast>
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-
CC       pass membrane protein.
else case <OC:Cyanobacteriota> and not <OC:Gloeobacter>
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane
CC       protein.
else case <OC:Gloeobacter>
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane
CC       protein.
else case not defined <Property:Membrane> or <Property:Membrane=1>
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
else case <Property:Membrane=2>
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane
CC       protein.
end case
case <OG:Chloroplast>
CC   -!- MISCELLANEOUS: In plastids the F-type ATPase is also known as
CC       CF(1)CF(0).
end case
CC   -!- SIMILARITY: Belongs to the ATPase B chain family.
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DR   Pfam; PF00430; ATP-synt_B; 1; trigger=no
DR   NCBIfam; TIGR01144; ATP_synt_b; 1; trigger=no
DR   General; Transmembrane; -; 1; trigger=yes
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KW   ATP synthesis
KW   CF(0)
KW   Hydrogen ion transport
KW   Ion transport
KW   Membrane
KW   Transmembrane
KW   Transport
case <OG:Chloroplast> or <OC:Cyanobacteriota> and not <OC:Gloeobacter>
KW   Thylakoid
else case <OC:Gloeobacter>
KW   Cell membrane
KW   Cell inner membrane
else case not defined <Property:Membrane> or <Property:Membrane=1>
KW   Cell membrane
else case <Property:Membrane=2>
KW   Cell membrane
KW   Cell inner membrane
end case
KW   Transmembrane helix
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GO   GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism
GO   GO:0015986; P:proton motive force-driven ATP synthesis
case <OC:Cyanobacteriota> and not <OC:Gloeobacter>
GO   GO:0042651; C:thylakoid membrane
else case <OG:Chloroplast>
GO   GO:0009535; C:chloroplast thylakoid membrane
else
GO   GO:0005886; C:plasma membrane
end case
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FT   None
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Size: 143-326;
Related: MF_01399!;
Template: P0ABA0; P09221; Q0ZS23; Q2RFX5; O05333;
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, CROS5, DESOH, DINSH, GLUOX, GRABC,
 MARMM, MARMS, CHESB, METCA, MYCA1, MYCA9, MYCBO, MYCBP, MYCGI, MYCLB, MYCLE,
 MYCMM, MYCPA, MYCS2, MYCSJ, MYCSK, MYCSS, MYCTA, MYCTU, MYCUA, MYCVP, NITMU,
 BRUA4, OCHNE, PARL1, SYNC1, CHLL3, PELPD, PROA2, PSEA6, PSEAE, RALN1, RHILO,
 RHOBA, RHOCS, ALBFT, STRPN, SYNAS, SYNP1, PICP2, SYNP6, SYNY3, VIBC1, VIBSP,
 XANP2
Plasmid: in ACAM1, PICP2
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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# Revision 1.36 2023/12/07
//