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Database: UniProt
Entry: Q85YC7_9VIRI
LinkDB: Q85YC7_9VIRI
Original site: Q85YC7_9VIRI 
ID   Q85YC7_9VIRI            Unreviewed;       399 AA.
AC   Q85YC7;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 98.
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:AAL92544.1};
OS   Coleochaete sp. 327d3.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AAL92544.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Coleochaetophyceae; Coleochaetales;
OC   Coleochaetaceae; Coleochaete.
OX   NCBI_TaxID=190328 {ECO:0000313|EMBL:AAL92544.1};
RN   [1] {ECO:0000313|EMBL:AAL92544.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=327d3 {ECO:0000313|EMBL:AAL92544.1};
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; AY082321; AAL92544.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q85YC7; -.
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:AAL92544.1};
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:AAL92544.1};
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:AAL92544.1"
FT   NON_TER         399
FT                   /evidence="ECO:0000313|EMBL:AAL92544.1"
SQ   SEQUENCE   399 AA;  43087 MW;  49458F9B23805424 CRC64;
     ILGDNKVRAV SMSATDGLMR GMDVIDTGAP LSVPVGEATL GRIFNVLGEP VDELGPVDST
     TTLPIHRSAP 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 RLTVARARKI
     ERFLSQPFFV AEVFTGSPGK YVSLIETIKG FQLILSGDL
//
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