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Database: UniProt
Entry: O98926_9CHLO
LinkDB: O98926_9CHLO
Original site: O98926_9CHLO 
ID   O98926_9CHLO            Unreviewed;       376 AA.
AC   O98926;
DT   01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=ATP synthase subunit beta {ECO:0000256|RuleBase:RU003553};
DE            EC=7.1.2.2 {ECO:0000256|RuleBase:RU003553};
DE   Flags: Fragment;
GN   Name=atpB {ECO:0000313|EMBL:BAA75581.1};
OS   Volvulina pringsheimii.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:BAA75581.1}.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Volvocaceae; Volvulina.
OX   NCBI_TaxID=47793 {ECO:0000313|EMBL:BAA75581.1};
RN   [1] {ECO:0000313|EMBL:BAA75581.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UTEX 1020 {ECO:0000313|EMBL:BAA75581.1};
RA   Nozaki H., Ohta N., Takano H., Watanabe M.M.;
RT   "Re-examination of phylogenetic relationships within the colonial
RT   Volvocales (Chlorophyta): an analysis of atpB and rbcL gene sequences.";
RL   J. Phycol. 35:104-112(1999).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. {ECO:0000256|RuleBase:RU003553}.
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|RuleBase:RU003553};
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).
CC       {ECO:0000256|RuleBase:RU003553}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936}.
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DR   EMBL; AB014028; BAA75581.1; -; Genomic_DNA.
DR   AlphaFoldDB; O98926; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
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-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
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; 3.40.50.12240; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR005722; ATP_synth_F1_bsu.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
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   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|ARBA:ARBA00023310,
KW   ECO:0000256|RuleBase:RU003553};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003553};
KW   CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|RuleBase:RU003553};
KW   Chloroplast {ECO:0000313|EMBL:BAA75581.1};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003553}; Plastid {ECO:0000313|EMBL:BAA75581.1};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          88..280
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAA75581.1"
FT   NON_TER         376
FT                   /evidence="ECO:0000313|EMBL:BAA75581.1"
SQ   SEQUENCE   376 AA;  40769 MW;  7A3389BE67B95980 CRC64;
     VSMNPTEGLM RGMEVLDTGK PLSVPVGKVT LGRIFNVLGE PVDNMGNVLI EDTLPIHRTA
     PAFVDLDTRL SIFETGIKVV DLLAPYRRGG KIGLFGGAGV GKTVLIMELI NNIAKAHGGV
     SVFAGVGERT REGNDLYTEM KESGVIVEKN LSDSKVALVY GQMNEPPGAR MRVALTALTM
     AEYFRDVNKQ DVLFFIDNIF RFVQAGAEVS ALLGRMPSAV GYQPTLATEM GGLQERITST
     KDGSITSIQA VYVPADDLTD PAPATTFAHL DATTVLSRNL AAKGIYPAVD PLESTSTMLQ
     PWIVGEKHYD SAQSVKKTLQ RYKELQDIIA ILGLDELSED DRLIVSRARK IERFLSQPFF
     VAEVFTGSPG KYVSLA
//
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