ATPBM_CHLRE
ID ATPBM_CHLRE Reviewed; 574 AA.
AC P38482;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=ATP synthase subunit beta, mitochondrial;
DE EC=7.1.2.2;
DE Flags: Precursor;
GN Name=ATP2;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1386535; DOI=10.1007/bf00027073;
RA Franzen L.-G., Falk G.;
RT "Nucleotide sequence of cDNA clones encoding the beta subunit of
RT mitochondrial ATP synthase from the green alga Chlamydomonas reinhardtii:
RT the precursor protein encoded by the cDNA contains both an N-terminal
RT presequence and a C-terminal extension.";
RL Plant Mol. Biol. 19:771-780(1992).
RN [2]
RP STRUCTURE BY NMR OF 1-26.
RX PubMed=8706917; DOI=10.1016/0014-5793(96)00734-x;
RA Lancelin J.-M., Gans P., Bouchayer E., Bally I., Arlaud G.J.,
RA Jacquot J.-P.;
RT "NMR structures of a mitochondrial transit peptide from the green alga
RT Chlamydomonas reinhardtii.";
RL FEBS Lett. 391:203-208(1996).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC Complex V) produces ATP from ADP in the presence of a proton gradient
CC across the membrane which is generated by electron transport complexes
CC of the respiratory chain. F-type ATPases consist of two structural
CC domains, F(1) - containing the extramembraneous catalytic core, and
CC F(0) - containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. Subunits alpha and
CC beta form the catalytic core in F(1). Rotation of the central stalk
CC against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of
CC ATP in three separate catalytic sites on the beta subunits.
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 three main
CC subunits: a, b and c.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC Note=Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; X61624; CAA43808.1; -; mRNA.
DR PIR; S23530; S23530.
DR RefSeq; XP_001691632.1; XM_001691580.1.
DR AlphaFoldDB; P38482; -.
DR SMR; P38482; -.
DR STRING; 3055.EDP04740; -.
DR PRIDE; P38482; -.
DR ProMEX; P38482; -.
DR EnsemblPlants; PNW69914; PNW69914; CHLRE_17g698000v5.
DR GeneID; 5717357; -.
DR Gramene; PNW69914; PNW69914; CHLRE_17g698000v5.
DR KEGG; cre:CHLRE_17g698000v5; -.
DR eggNOG; KOG1350; Eukaryota.
DR HOGENOM; CLU_022398_0_2_1; -.
DR OMA; GFNMIMD; -.
DR OrthoDB; 495235at2759; -.
DR GO; GO:0005743; C:mitochondrial inner 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-KW.
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 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; 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 Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01039; atpD; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW ATP synthesis; ATP-binding; CF(1); Hydrogen ion transport; Ion transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Transit peptide; Translocase; Transport.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..574
FT /note="ATP synthase subunit beta, mitochondrial"
FT /id="PRO_0000002436"
FT BINDING 183..190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 574 AA; 61821 MW; 22B3C6C6D18FBCFE CRC64;
MLSSVRLAAL RAGKTNSVFQ AVRAFAAEPA AAATTDAGFV SQVIGPVVDV RFDGELPSIL
SALEVQGHNV RLVLEVAQHM GDNTVRCVAM DSTDGLVRGQ KVVNTGSPIK VPVGRGTLGR
IMNVIGEPVD EQGPIECSEV WSIHREAPEF TEQSTEQEIL VTGIKVVDLL APYQRGGKIG
LFGGAGVGKT VLIMELINNV AKAHGGFSVF AGVGERTREG NDLYREMIES GVIKLGDKRG
ESKCTLVYGQ MNEPPGARAR VALTGLTVAE YFRDVEGQDV LLFVDNIFRF TQANSEVSAL
LGRIPSAVGY QPTLATDLGG LQERITTTTK GSITSVQAVY VPADDLTDPA PATTFAHLDA
TTVLSRSIAE LGIYPAVDPL DSTSRMLNPN IIGAEHYNIA RGVQKVLQDY KNLQDIIAIL
GMDELSEEDK LTVARARKIQ RFLSQPFQVA EVFTGTPGKY VDLKDTISAF TGILQGKYDD
LPEMAFYMVG GIHEVVEKAD KLAKDVAARK DESKKAKSSE ALKDVPSLEK MAGEIKDEVI
DADDSLEEDF KAEAISSENM VLNEKGEKVP LPKK
