ATPBM_NICPL
ID ATPBM_NICPL Reviewed; 560 AA.
AC P17614;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=ATP synthase subunit beta, mitochondrial;
DE EC=7.1.2.2;
DE Flags: Precursor;
GN Name=ATPB; Synonyms=ATP2-1;
OS Nicotiana plumbaginifolia (Leadwort-leaved tobacco) (Tex-Mex tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4092;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2866954; DOI=10.1002/j.1460-2075.1985.tb03910.x;
RA Boutry M., Chua N.H.;
RT "A nuclear gene encoding the beta subunit of the mitochondrial ATP synthase
RT in Nicotiana plumbaginifolia.";
RL EMBO J. 4:2159-2165(1985).
RN [2]
RP STRUCTURE BY NMR OF 1-54, AND TRANSIT PEPTIDE CLEAVAGE SITE.
RX PubMed=15037074; DOI=10.1016/j.jmb.2004.01.006;
RA Moberg P., Nilsson S., Staehl A., Eriksson A.-C., Glaser E., Maeler L.;
RT "NMR solution structure of the mitochondrial F1beta presequence from
RT Nicotiana plumbaginifolia.";
RL J. Mol. Biol. 336:1129-1140(2004).
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 -!- INTERACTION:
CC P17614; Q9LJL3: PREP1; Xeno; NbExp=6; IntAct=EBI-7143406, EBI-7143359;
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}.
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 EMBL; X02868; CAA26620.1; -; Genomic_DNA.
DR PIR; A24355; A24355.
DR PDB; 1PYV; NMR; -; A=1-54.
DR PDBsum; 1PYV; -.
DR AlphaFoldDB; P17614; -.
DR SMR; P17614; -.
DR IntAct; P17614; 1.
DR MINT; P17614; -.
DR PRIDE; P17614; -.
DR EvolutionaryTrace; P17614; -.
DR GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IEA:InterPro.
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 Gene3D; 1.10.10.910; -; 1.
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; IPR042079; ATP_synt_F1_beta_sf.
DR InterPro; IPR020971; ATP_synth_F1_beta_su.
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 Pfam; PF11421; Synthase_beta; 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 3D-structure; ATP synthesis; ATP-binding; CF(1); Hydrogen ion transport;
KW Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotide-binding; Transit peptide; Translocase; Transport.
FT TRANSIT 1..54
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:15037074"
FT CHAIN 55..560
FT /note="ATP synthase subunit beta, mitochondrial"
FT /id="PRO_0000002440"
FT REGION 20..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 235..242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT HELIX 5..15
FT /evidence="ECO:0007829|PDB:1PYV"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:1PYV"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:1PYV"
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:1PYV"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:1PYV"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:1PYV"
SQ SEQUENCE 560 AA; 59856 MW; 7A00781A5021063A CRC64;
MASRRLLASL LRQSAQRGGG LISRSLGNSI PKSASRASSR ASPKGFLLNR AVQYATSAAA
PASQPSTPPK SGSEPSGKIT DEFTGAGSIG KVCQVIGAVV DVRFDEGLPP ILTALEVLDN
QIRLVLEVAQ HLGENMVRTI AMDGTEGLVR GQRVLNTGSP ITVPVGRATL GRIINVIGEA
IDERGPITTD HFLPIHREAP AFVEQATEQQ ILVTGIKVVD LLAPYQRGGK IGLFGGAGVG
KTVLIMELIN NVAKAHGGFS VFAGVGERTR EGNDLYREMI ESGVIKLGEK QSESKCALVY
GQMNEPPGAR ARVGLTGLTV AEHFRDAEGQ DVLLFIDNIF RFTQANSEVS ALLGRIPSAV
GYQPTLATDL GGLQERITTT KKGSITSVQA IYVPADDLTD PAPATTFAHL DATTVLSRQI
SELGIYPAVD PLDSTSRMLS PHILGEDHYN TARGVQKVLQ NYKNLQDIIA ILGMDELSED
DKMTVARARK IQRFLSQPFH VAEVFTGAPG KYVDLKESIN SFQGVLDGKY DDLSEQSFYM
VGGIDEVIAK AEKIAKESAA
