ATPB_MICAN
ID ATPB_MICAN Reviewed; 482 AA.
AC B0JFM7;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=ATP synthase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
DE AltName: Full=F-ATPase subunit beta {ECO:0000255|HAMAP-Rule:MF_01347};
GN Name=atpD {ECO:0000255|HAMAP-Rule:MF_01347};
GN Synonyms=atpB {ECO:0000255|HAMAP-Rule:MF_01347};
GN OrderedLocusNames=MAE_00920;
OS Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Microcystaceae; Microcystis.
OX NCBI_TaxID=449447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-843 / IAM M-247;
RX PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT Microcystis aeruginosa NIES-843.";
RL DNA Res. 14:247-256(2007).
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. {ECO:0000255|HAMAP-Rule:MF_01347}.
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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01347};
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). {ECO:0000255|HAMAP-
CC Rule:MF_01347}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01347}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01347}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01347}.
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DR EMBL; AP009552; BAF99913.1; -; Genomic_DNA.
DR RefSeq; WP_012263845.1; NC_010296.1.
DR AlphaFoldDB; B0JFM7; -.
DR SMR; B0JFM7; -.
DR STRING; 449447.MAE_00920; -.
DR PaxDb; B0JFM7; -.
DR PRIDE; B0JFM7; -.
DR EnsemblBacteria; BAF99913; BAF99913; MAE_00920.
DR KEGG; mar:MAE_00920; -.
DR PATRIC; fig|449447.4.peg.84; -.
DR eggNOG; COG0055; Bacteria.
DR HOGENOM; CLU_022398_0_2_3; -.
DR OMA; GFNMIMD; -.
DR OrthoDB; 430176at2; -.
DR BioCyc; MAER449447:MAE_RS00390-MON; -.
DR Proteomes; UP000001510; Chromosome.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005722; ATP_synth_F1_bsu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01039; atpD; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis; ATP-binding; CF(1); Hydrogen ion transport; Ion transport;
KW Membrane; Nucleotide-binding; Reference proteome; Thylakoid; Translocase;
KW Transport.
FT CHAIN 1..482
FT /note="ATP synthase subunit beta"
FT /id="PRO_0000339546"
FT BINDING 161..168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01347"
SQ SEQUENCE 482 AA; 51614 MW; F85A2920B43E215D CRC64;
MVATTETNVG KIVQIIGPVI DAEFPSGKLP RIYNALTVKG TNSAGQNLSV TCEVQQLLGD
NQVRAVAMST TDGLVRGMDI VDTGAAISVP VGKCTLGRIF NVLGEPVDEK GPVNVTETSP
IHRPAPKLVD LEVTPTVFET GIKVIDLLTP YRQGGKIGLF GGAGVGKTVI MMELINNIAI
QHGGVSVFGG VGERTREGND LYNEMIESKV INADNPEDSK IALVYGQMNE PPGARMRVGL
SALTMAEYFR DVSKQDVLLF IDNIFRFVQA GSEVSALLGR MPSAVGYQPT LGTDVGDLQE
RITSTKEGSI TSIQAVYVPA DDLTDPAPAT TFAHLDGTTV LSRGLASKGI YPAVDPLGST
STMLQADIVG DEHYGTARAV QSTLQRYKEL QDIIAILGLD ELSEEDRLTV DRARKIERFL
SQPFFVAEVF TGSPGKYVTL ADTIKGFQMI LKGELDSLPE QAFYMVGSID EAIAKGEKLK
KG
