AC MF_01347; DC Protein; auto c? or TR HAMAP; MF_01347; -; 1; level=0 XX Names: ATP_synth_beta_bact XX ID ATPB case DE RecName: Full=ATP synthase subunit beta; DE EC=7.1.2.2; DE AltName: Full=ATP synthase F1 sector subunit beta; DE AltName: Full=F-ATPase subunit beta; else case DE RecName: Full=ATP synthase subunit beta, chloroplastic; DE EC=7.1.2.2; DE AltName: Full=ATP synthase F1 sector subunit beta; DE AltName: Full=F-ATPase subunit beta; end case case GN Name=atpB; else case GN Name=atpD; Synonyms=atpB; else GN Name=atpD; end case XX CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient CC across the membrane. The catalytic sites are hosted primarily by the CC beta subunits. 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 or 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(1), b(1), b'(1) and c(9-12). 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 CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; CC Peripheral membrane protein. else case and not CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane CC protein. else case CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. else case not defined or CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. else case 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; TIGR01039; AtpD; 1; trigger=no XX KW ATP synthesis KW ATP-binding KW CF(1) KW Hydrogen ion transport KW Ion transport KW Nucleotide-binding KW Translocase KW Transport KW Membrane case or and not KW Thylakoid else case KW Cell membrane KW Cell inner membrane else case not defined or KW Cell membrane else case 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 and not GO GO:0042651; C:thylakoid membrane else case GO GO:0009535; C:chloroplast thylakoid membrane else GO GO:0005886; C:plasma membrane end case XX FT From: ATPB_ECOLI (P0ABB4) FT BINDING 150..157 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: G-G-A-G-[V,L,C,M]-G-K-[T,S] XX Size: 447-542; Related: None; Template: P0ABB4; Scope: Bacteria Plastid Fusion: Nter: Cter: None Duplicate: in BRASB, BURM7, BURMA, BURMS, BURP0, BURP1, BURP6, BURPS, PARXL, CHLTE, DINSH, GLUOX, LISIN, LISMF, LISMO, LISW6, MARMS, MYCPU, NITEC, NITMU, SYNC1, CHLL3, PELPD, PHOPR, POLNA, PSEA6, PSYIN, ALBFT, CERS1, SHEFN, VIBC1 Plasmid: in CERS1, CERS4 Comments: Fused with an unknown domain in MALP2. Some of the Rhizobiales have a slightly longer N-terminus. XX # Revision 1.53 2023/06/01 //