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Database: UniProt
Entry: Q85YC8_9VIRI
LinkDB: Q85YC8_9VIRI
Original site: Q85YC8_9VIRI 
ID   Q85YC8_9VIRI            Unreviewed;       396 AA.
AC   Q85YC8;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 96.
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:AAL92543.1};
OS   Coleochaete pulvinata.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AAL92543.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Coleochaetophyceae; Coleochaetales;
OC   Coleochaetaceae; Coleochaete.
OX   NCBI_TaxID=173054 {ECO:0000313|EMBL:AAL92543.1};
RN   [1] {ECO:0000313|EMBL:AAL92543.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=56a6 {ECO:0000313|EMBL:AAL92543.1};
RA   Cimino M.T., Delwiche C.F.;
RT   "Molecular and morphological data identify a cryptic species complex in
RT   endophytic members of the genus Coleochaete Breb (Chlorophyta:
RT   Coleochaetaceae).";
RL   J. Phycol. 38:1213-1221(2002).
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|ARBA:ARBA00001741,
CC         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; AY082320; AAL92543.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q85YC8; -.
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; 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; 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   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.
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:AAL92543.1};
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:AAL92543.1};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          97..289
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAL92543.1"
FT   NON_TER         396
FT                   /evidence="ECO:0000313|EMBL:AAL92543.1"
SQ   SEQUENCE   396 AA;  42832 MW;  605DB6978478A6E1 CRC64;
     ILGDNKVRAV SMSATDGLMR GMDAIDTGAP LSVPVGEVTL GRIFNVLGEP VDELGPVDST
     VTFPIHRSAP AFTQLDTKLS IFETGIKVVD LLAPYRRGGK IGLFGGAGVG KTVLIMELIN
     NIAKAHGGVS VFGGVGERTR EGNDLYMEMK ESKVINEENI SESKVALVYG QMNEPPGARM
     RVGLTALTMA EYFRDVNKQD VLLFIDNIFR FVQAGSEVSA LLGRMPSAVG YQPTLSTEMG
     TLQERITSTK EGSITSIQAV YVPADDLTDP APATTFAHLD ATTVLSRGLA AKGIYPAVDP
     LDSTSTMLQP WIVGQEHYET AQGVKQTLQR YKELQDIIAI LGLDELSEED RLIVARARKI
     ERFLSQPFFV AEVFTGSPGK YVSLVETIKG FQLILS
//
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