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Database: UniProt
Entry: A0A2A2TDZ3_9CYAN
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ID   A0A2A2TDZ3_9CYAN        Unreviewed;       478 AA.
AC   A0A2A2TDZ3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=ATP synthase subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
DE            EC=7.1.2.2 {ECO:0000256|HAMAP-Rule:MF_01347};
DE   AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
DE   AltName: Full=F-ATPase subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
GN   Name=atpD {ECO:0000256|HAMAP-Rule:MF_01347};
GN   Synonyms=atpB {ECO:0000256|HAMAP-Rule:MF_01347};
GN   ORFNames=CK510_22005 {ECO:0000313|EMBL:PAX51952.1};
OS   Calothrix elsteri CCALA 953.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC   Calothrix.
OX   NCBI_TaxID=987040 {ECO:0000313|EMBL:PAX51952.1, ECO:0000313|Proteomes:UP000218238};
RN   [1] {ECO:0000313|EMBL:PAX51952.1, ECO:0000313|Proteomes:UP000218238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCALA 953 {ECO:0000313|EMBL:PAX51952.1,
RC   ECO:0000313|Proteomes:UP000218238};
RA   Gagunashvili A.N., Elster J., Andresson O.S.;
RT   "Draft genome sequence of filamentous cyanobacterium Calothrix elsteri
RT   CCALA 953.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_01347};
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01347}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01347}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_01347}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PAX51952.1}.
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DR   EMBL; NTFS01000305; PAX51952.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2TDZ3; -.
DR   OrthoDB; 9801639at2; -.
DR   Proteomes; UP000218238; Unassembled WGS sequence.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   CDD; cd18110; ATP-synt_F1_beta_C; 1.
DR   CDD; cd01133; F1-ATPase_beta_CD; 1.
DR   Gene3D; 2.40.10.170; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; 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   NCBIfam; TIGR03305; alt_F1F0_F1_bet; 1.
DR   NCBIfam; TIGR01039; atpD; 1.
DR   PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR   PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR   SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW   Rule:MF_01347};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01347};
KW   CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|HAMAP-Rule:MF_01347};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01347};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_01347};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01347};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01347}; Reference proteome {ECO:0000313|Proteomes:UP000218238};
KW   Thylakoid {ECO:0000256|HAMAP-Rule:MF_01347};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW   Rule:MF_01347};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01347}.
FT   DOMAIN          156..341
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   BINDING         164..171
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   478 AA;  52196 MW;  815AFCBDA06615C3 CRC64;
     MEPNIKSSSQ SNHSQEQNLG SILSVRSSII DIHFPKRLPY INSQLKTGKG GNLSIEVVSH
     LSAQVVRGVA LAPTAGLTRG EVVIDTQHPL QVPVGDRLLG RMLNLFGEVI DEKEAIAGGE
     WRSIHATPIA MSERVTKAEI LKTGIKAIDL LTPLERGGKT GLLGGAGVGK TVLITEMIHN
     MVKQQQGVSL FCGIGERCRE GLDLYQEMQA TGVLPNAVLV FGQMNEPPGV RFWVGHAALT
     MAEYFRDRSQ KDVLLLIDNI FRFIQAGSEV SGLMGILPSR VGYEPTLATE LAQLEERICN
     TSAGAITSIQ AVYVPADDFT DPSAVAVFSH LSASIVLSRK RASEGLYPAV DLMQSNSKML
     MPHIVGDRHY QIAQAVRKTI STYEELKDII AMLGLEELSS GDRQVVSQAR RLERFLTQPF
     FSTAQFTGLT GKLVELDDAL KGCERILNDE FADTPERSLY MIGSIDEVVK VPKEDKKS
//
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