ID   ATPB_ACAM1              Reviewed;         456 AA.
AC   A8ZNR6;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 90.
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;
GN   Name=atpD; Synonyms=atpB; OrderedLocusNames=AM1_D0157;
OS   Acaryochloris marina (strain MBIC 11017).
OG   Plasmid pREB4.
OC   Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
OC   Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBIC 11017;
RX   PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA   Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA   Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA   Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA   Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA   Blankenship R.E., Touchman J.W.;
RT   "Niche adaptation and genome expansion in the chlorophyll d-producing
RT   cyanobacterium Acaryochloris marina.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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 (By similarity). {ECO:0000250}.
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   -!- 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) (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; CP000841; ABW32652.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8ZNR6; -.
DR   SMR; A8ZNR6; -.
DR   EnsemblBacteria; ABW32652; ABW32652; AM1_D0157.
DR   KEGG; amr:AM1_D0157; -.
DR   HOGENOM; CLU_022398_0_2_3; -.
DR   OMA; MLFGQMN; -.
DR   Proteomes; UP000000268; Plasmid pREB4.
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; IPR017691; Alt_ATPase_F1_bsu.
DR   InterPro; IPR005722; ATP_synth_F1_bsu.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
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   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR03305; alt_F1F0_F1_bet; 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; Plasmid; Reference proteome; Thylakoid;
KW   Translocase; Transport.
FT   CHAIN           1..456
FT                   /note="ATP synthase subunit beta"
FT                   /id="PRO_0000339466"
FT   BINDING         135..142
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   456 AA;  49671 MW;  5BBB8A47AC419A34 CRC64;
     MVDVHFSDEV PPLRHLLRAG PQAQIAIEGL TYLSANLIRG IALTPTQGLA RGARVIDTGQ
     SLQVPIGEHL LGRAFNVFGD PIDGLGPLKG MKRSLHGQAV PLHQRTTGTD ILVTGIKAID
     LLAPLERGSK AGLFGGAGVG KTVLITEMIH NIVSRYDGVS IFCGIGERSR EGEELYREMK
     AAGVLNNTVM VFGQMNEPPG SRFRVGHAAL TMAEYFRDQA HRDVLLMIDN VFRFIQAGSE
     VSGLMGQLPS RVGYQPTLAT ELAELEERIC STAHGAITSV QAVYIPADDL TDPAAVHTFS
     HLSASIVLSR KRTSEGLYPA VDPLQSGSKM LTPSVVGQRH YQVAQAVRKT LAEYEDLKDI
     IAMLGLEELA QNERQTVYRA RRLERFLTQP FFTTEQFSGI PGKMVSLDQT LTGCEAILDD
     KCSGLSEQAL YMIGAVDEAE LEHQEREAQE VEEIGQ