ATPB_TRYBB
ID ATPB_TRYBB Reviewed; 519 AA.
AC Q9GPE9; A0A2U3T1M9;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=ATP synthase subunit beta, mitochondrial;
DE EC=7.1.2.2 {ECO:0000255|RuleBase:RU003553, ECO:0000305|PubMed:29247468};
DE AltName: Full=ATP synthase F1 subunit beta {ECO:0000303|PubMed:19436713};
DE Flags: Precursor;
GN ORFNames=Tb427.03.1380 {ECO:0000303|PubMed:19436713};
OS Trypanosoma brucei brucei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=5702 {ECO:0000312|EMBL:AAG23340.1};
RN [1] {ECO:0000312|EMBL:AAG23340.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-40, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RC STRAIN=Treu 667 {ECO:0000303|PubMed:11295183};
RX PubMed=11295183; DOI=10.1016/s0166-6851(01)00233-x;
RA Brown S.V., Stanislawski A., Perry Q.L., Williams N.;
RT "Cloning and characterization of the subunits comprising the catalytic core
RT of the Trypanosoma brucei mitochondrial ATP synthase.";
RL Mol. Biochem. Parasitol. 113:289-301(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF
RP 22-519 IN COMPLEX WITH ATP, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=427;
RX PubMed=29440423; DOI=10.1073/pnas.1720940115;
RA Montgomery M.G., Gahura O., Leslie A.G.W., Zikova A., Walker J.E.;
RT "ATP synthase from Trypanosoma brucei has an elaborated canonical F1-domain
RT and conventional catalytic sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:2102-2107(2018).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND NOMENCLATURE.
RC STRAIN=427;
RX PubMed=19436713; DOI=10.1371/journal.ppat.1000436;
RA Zikova A., Schnaufer A., Dalley R.A., Panigrahi A.K., Stuart K.D.;
RT "The F(0)F(1)-ATP synthase complex contains novel subunits and is essential
RT for procyclic Trypanosoma brucei.";
RL PLoS Pathog. 5:E1000436-E1000436(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PROTEIN SEQUENCE OF 22-26, SUBCELLULAR
RP LOCATION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=427;
RX PubMed=29247468; DOI=10.1111/febs.14364;
RA Gahura O., Subrtova K., Vachova H., Panicucci B., Fearnley I.M.,
RA Harbour M.E., Walker J.E., Zikova A.;
RT "The F1-ATPase from Trypanosoma brucei is elaborated by three copies of an
RT additional p18-subunit.";
RL FEBS J. 285:614-628(2018).
CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(o) ATP synthase)
CC produces ATP from ADP in the presence of a proton gradient across the
CC membrane which is generated by electron transport complexes of the
CC respiratory chain (PubMed:19436713, PubMed:29247468). F-type ATPases
CC consist of two structural domains, F(1) - containing the
CC extramembraneous catalytic core, and F(o) - containing the membrane
CC proton channel, linked together by a central stalk and a peripheral
CC stalk (PubMed:19436713, PubMed:29247468, PubMed:29440423). During
CC catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via
CC a rotary mechanism of the central stalk subunits to proton
CC translocation. Subunits alpha and beta form the catalytic core in F(1)
CC (PubMed:19436713, PubMed:29440423). 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 (Probable).
CC Contrary to the procyclic, insect form that requires F(1)F(o) ATP
CC synthase for ATP synthesis, the bloodstream form relies on ATP
CC hydrolysis by F(1)F(o) ATP synthase to maintain its mitochondrial
CC membrane potential (PubMed:29247468). {ECO:0000269|PubMed:19436713,
CC ECO:0000269|PubMed:29247468, ECO:0000269|PubMed:29440423, ECO:0000305}.
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|RuleBase:RU003553,
CC ECO:0000305|PubMed:29247468};
CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC - and F(o) - the membrane proton channel. F(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1), plus the additional
CC subunit P18 (Tb427.05.1710) that is not present in F(1)F(o) ATP
CC synthase from metazoa (PubMed:19436713, PubMed:29247468,
CC PubMed:29440423). Subunit P18 (Tb927.5.1710) interacts with the alpha
CC subunit with a 1:1 stoichiometry; the interaction is direct
CC (PubMed:29440423). Subunit gamma is part of the central stalk
CC (PubMed:29440423). F(o) has three main subunits: a, b and c
CC (PubMed:19436713). The trypanosomal ATPase complex contains additional
CC subunits that are not present in the F(1)F(o) ATP synthase from metazoa
CC (PubMed:19436713, PubMed:29247468, PubMed:29440423).
CC {ECO:0000269|PubMed:19436713, ECO:0000269|PubMed:29247468,
CC ECO:0000269|PubMed:29440423}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane
CC {ECO:0000269|PubMed:11295183, ECO:0000269|PubMed:19436713,
CC ECO:0000269|PubMed:29247468, ECO:0000269|PubMed:29440423}; Peripheral
CC membrane protein {ECO:0000269|PubMed:11295183,
CC ECO:0000269|PubMed:19436713, ECO:0000269|PubMed:29247468,
CC ECO:0000269|PubMed:29440423}; Matrix side {ECO:0000305|PubMed:19436713,
CC ECO:0000305|PubMed:29247468, ECO:0000305|PubMed:29440423}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; AY007706; AAG23340.1; -; mRNA.
DR EMBL; LS423644; SPS16790.1; -; Genomic_DNA.
DR PDB; 6F5D; X-ray; 3.20 A; D/E/F=22-519.
DR PDBsum; 6F5D; -.
DR AlphaFoldDB; Q9GPE9; -.
DR SMR; Q9GPE9; -.
DR TCDB; 3.A.2.1.13; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR OMA; GFNMIMD; -.
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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; ATP-binding; CF(1); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Transit peptide;
KW Translocase; Transport.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:11295183,
FT ECO:0000269|PubMed:29247468"
FT CHAIN 22..519
FT /note="ATP synthase subunit beta, mitochondrial"
FT /id="PRO_0000444142"
FT BINDING 184..191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:29440423,
FT ECO:0007744|PDB:6F5D"
FT BINDING 216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00829"
FT CONFLICT 441..447
FT /note="SQPFQVA -> PAIPSC (in Ref. 1; AAG23340)"
SQ SEQUENCE 519 AA; 55776 MW; 9065D1C48BF9AF80 CRC64;
MLTRFRSAVL RGAVSITGAR AASTAPVADH KGRVGHVSQV IGAVVDVHFA DGVPPVLTAL
DVVDKLGRDE PLTLEIVQHL DAHTGRCIAM QTTDLLKLKA KVVSTGGNIS VPVGRETLGR
IFNVLGDAID QRGPVGEKLR MPIHAVAPKL ADQAAEDAVL TTGIKVIDLI LPYCKGGKIG
LFGGAGVGKT VIIMELINNV AKGHGGFSVF AGVGERTREG TDLYLEMMQS KVIDLKGESK
CVLVYGQMNE PPGARARVAQ SALTMAEYFR DVEGQDVLLF IDNIFRFTQA NSEVSALLGR
IPAAVGYQPT LAEDLGQLQE RITSTTKGSI TSVQAVYVPA DDITDPAPAT TFSHLDATTV
LDRAVAESGI YPAVNPLECA SRIMDPDVIS VDHYNVAQDV VQMLTKYREL QDIIAVLGID
ELSEEDKLIV DRARKLVKFL SQPFQVAEVF TGMTGHYVQL DDTIDSFSGL LMGTYDQVPE
MAFYMVGGIN SVLEKAKKMA EEAAELEKMR RARVAQASS
