AC   MF_01346;
DC   Protein; auto
c?   <OC:Bacteria> or <OG:Chloroplast>
TR   HAMAP; MF_01346; -; 1; level=0
XX
Names: ATP_synth_alpha_bact
XX
ID   ATPA
case <OC:Bacteria>
DE   RecName: Full=ATP synthase subunit alpha;
DE            EC=7.1.2.2;
DE   AltName: Full=ATP synthase F1 sector subunit alpha;
DE   AltName: Full=F-ATPase subunit alpha;
else case <OG:Chloroplast>
DE   RecName: Full=ATP synthase subunit alpha, chloroplastic;
DE            EC=7.1.2.2;
DE   AltName: Full=ATP synthase F1 sector subunit alpha;
DE   AltName: Full=F-ATPase subunit alpha;
end case
GN   Name=atpA;
XX
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The alpha chain is a regulatory subunit.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
case <OG:Chloroplast> or <Property:PHOTOSYN>
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main
CC       subunits: a, b, b' and c.
else
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC       subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an
CC       alternating ring which encloses part of the gamma chain. CF(1) is
CC       attached to CF(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;
CC       Peripheral membrane protein.
else case <OC:Cyanobacteriota> and not <OC:Gloeobacter>
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane
CC       protein.
else case <OC:Gloeobacter>
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein.
else case not defined <Property:Membrane> or <Property:Membrane=1>
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
else case <Property:Membrane=2>
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein.
end case
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
XX
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1; trigger=no
DR   Pfam; PF00006; ATP-synt_ab; 1; trigger=no
DR   Pfam; PF00306; ATP-synt_ab_C; 1; trigger=no
DR   Pfam; PF02874; ATP-synt_ab_N; 1; trigger=no
DR   NCBIfam; TIGR00962; AtpA; 1; trigger=no
XX
KW   ATP synthesis
KW   ATP-binding
KW   CF(1)
KW   Ion transport
KW   Nucleotide-binding
KW   Translocase
KW   Transport
KW   Hydrogen ion transport
KW   Membrane
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
XX
GO   GO:0005524; F:ATP binding
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
XX
FT   From: ATPA_ECOLI (P0ABB0)
FT   BINDING         169..176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-D-[R,K,S]-[Q,A,K,S,G]-[T,I,C,V]-G-K-[T,S,A]
FT   SITE            373
FT                   /note="Required for activity"
FT   Condition: S
XX
Size: 481-670;
Related: None;
Template: P0ABB0;
Scope:
 Bacteria
 Plastid
Fusion:
 Nter: None
 Cter: <Unknown>
Duplicate: in BURM7, BURMA, BURMS, BURP0, BURP1, BURP6, BURPS, BURTA, BURXA,
 PARXL, DINSH, GLUOX, HAHCH, LEGPA, LEGPC, LEGPH, LISIN, LISMF, LISMO, LISW6,
 MARMS, METCA, MYCPU, NITEC, NITMU, SYNC1, CHLL3, PELPD, PHOPR, POLNA, PSEA6,
 PSYIN, RHOBA, ALBFT, CERS1, SHEFN, SYNAS, VIBC1
Plasmid: in ACAM1, CERS1, CERS4
Comments: The second copy in some of the Burkholderia is quite a bit longer.
 There is a 250 residue fusion of unknown function in UREPA and UREP2.
XX
# Revision 1.57 2023/06/01
//