ID   ATPBM_VITSX             Reviewed;          62 AA.
AC   P85088;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=ATP synthase subunit beta, mitochondrial;
DE            EC=7.1.2.2;
DE   Flags: Fragments;
OS   Vitis sp. (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis; unclassified Vitis.
OX   NCBI_TaxID=3604;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND INDUCTION.
RC   STRAIN=V.simpsonii cv. Pixiola X V.vinifera cv. Golden Muscat
RC   {ECO:0000269|PubMed:18931950}; TISSUE=Leaf {ECO:0000269|PubMed:18931950};
RX   PubMed=18931950; DOI=10.1007/s12010-008-8380-3;
RA   Vasanthaiah H.K.N., Katam R., Basha S.M.;
RT   "Characterization of unique and differentially expressed proteins in
RT   anthracnose-tolerant Florida hybrid bunch grapes.";
RL   Appl. Biochem. Biotechnol. 157:395-406(2009).
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         Evidence={ECO:0000255|PROSITE-ProRule:PRU10106, ECO:0000305};
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. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. Mitochondrion inner
CC       membrane. Note=Peripheral membrane protein.
CC   -!- INDUCTION: By E.ampelina infection. {ECO:0000269|PubMed:18931950}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P85088; -.
DR   SMR; P85088; -.
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   InterPro; IPR027417; P-loop_NTPase.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   ATP synthesis; ATP-binding; CF(1); Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..>62
FT                   /note="ATP synthase subunit beta, mitochondrial"
FT                   /id="PRO_0000283823"
FT   NON_CONS        14..15
FT                   /evidence="ECO:0000303|PubMed:18931950"
FT   NON_CONS        27..28
FT                   /evidence="ECO:0000303|PubMed:18931950"
FT   NON_TER         62
FT                   /evidence="ECO:0000303|PubMed:18931950"
SQ   SEQUENCE   62 AA;  6434 MW;  3A485C30A4BD60F5 CRC64;
     VLNTGSPITV PVGRVGLTGL TVAEHFRFTQ ANSEVSALLG RIPSAVGYQP TLATDLGGLQ
     ER