ATPA_TRYBB
ID ATPA_TRYBB Reviewed; 584 AA.
AC Q9GS23; A0A2U3T1N3;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=ATP synthase subunit alpha, mitochondrial {ECO:0000305|PubMed:19436713};
DE AltName: Full=ATP synthase F1 subunit alpha {ECO:0000303|PubMed:19436713};
DE Flags: Precursor;
GN ORFNames=Tb427.07.7420, Tb427.07.7430 {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:AAG23339.1};
RN [1] {ECO:0000312|EMBL:AAG23339.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 160-175, SUBCELLULAR
RP LOCATION, SUBUNIT, AND PROTEOLYTIC CLEAVAGE.
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 25-584 IN COMPLEX WITH ADP, 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, DISRUPTION PHENOTYPE, 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, DISRUPTION PHENOTYPE, PROTEIN SEQUENCE OF 25-29 AND 160-165,
RP SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP PROTEOLYTIC CLEAVAGE.
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 Subunit alpha does not bear the catalytic high-affinity ATP-binding
CC sites (PubMed:29440423). Contrary to the procyclic, insect form that
CC requires F(1)F(o) ATP synthase for ATP synthesis, the bloodstream form
CC relies on ATP hydrolysis by F(1)F(o) ATP synthase to maintain its
CC mitochondrial membrane potential (PubMed:29247468).
CC {ECO:0000269|PubMed:19436713, ECO:0000269|PubMed:29247468,
CC ECO:0000269|PubMed:29440423, ECO:0000305}.
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 -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown of the protein in
CC procyclic, insect stage cells impairs assembly of the F(1) component
CC and slows the proliferation rate of procyclic cells that are cultivated
CC in vitro, both in the presence and in the absence of glucose in the
CC growth medium. ATP synthesis by oxidative phosphorylation is
CC dramatically reduced in procyclic cells. {ECO:0000269|PubMed:19436713,
CC ECO:0000269|PubMed:29247468}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; AY007705; AAG23339.1; -; mRNA.
DR EMBL; LS423643; SPS16789.1; -; Genomic_DNA.
DR PDB; 6F5D; X-ray; 3.20 A; A/B/C=25-584.
DR PDBsum; 6F5D; -.
DR AlphaFoldDB; Q9GS23; -.
DR SMR; Q9GS23; -.
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; QDKCDSS; -.
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:InterPro.
DR CDD; cd01132; F1_ATPase_alpha; 1.
DR InterPro; IPR000793; ATP_synth_asu_C.
DR InterPro; IPR033732; ATP_synth_F1_a.
DR InterPro; IPR005294; ATP_synth_F1_asu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00962; atpA; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 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 Transport.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:29247468"
FT CHAIN 25..584
FT /note="ATP synthase subunit alpha, mitochondrial"
FT /id="PRO_5004326611"
FT BINDING 207..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:29440423,
FT ECO:0007744|PDB:6F5D"
FT BINDING 464
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:29440423,
FT ECO:0007744|PDB:6F5D"
FT SITE 159..160
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:11295183,
FT ECO:0000269|PubMed:29247468"
FT SITE 407
FT /note="Required for activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10106"
FT CONFLICT 205
FT /note="V -> CN (in Ref. 1; AAG23339)"
FT CONFLICT 466
FT /note="Q -> H (in Ref. 1; AAG23339)"
SQ SEQUENCE 584 AA; 63503 MW; 3EC9E191E278F565 CRC64;
MRRFGSKFAS GLASRCALAC PLASAATAPA GASTTSSTSS AQKSFFKTTE MIGYVHSIDG
TIATLIPAPG NPGVAYNTII QIQVSPTTFA AGLVFNLEKD GRIGIILMDN ITEVQSGQKV
MATGQLLHIP VGAGVLGKVV NPLGHEVPVG LVTRSRRLLD STLGKVDTGA PNIVSRSPVN
YNLLTGFKAV DTMIPIGRGQ RELIVGDRQT GKTSIAVSTI INQVRINQQI LSKNAVISIY
VSIGQRCSNV ARIHRLLQSY GALRYTTVMA ATAAEPAGLQ YLAPYAGVTM GEYFMNRGRH
CLCVYDDLSK QAVAYRQISL LLRRPPGREA YPGDVFYLHS RLLERAAMLS PGKGGGSVTA
LPIVETLSND VTAYIVTNVI SITDGQIYLD TKLFTGGQRP AVNIGLSVSR VGSSAQNAAM
KGVAGKLKGI LAEYRKLAAD SVGGQQVQTI PMIRGARFVA LFNQKQPSYF MNAIVSLYAC
LNGYLDDVKV QYVKFYEYLL VHRDLGIMYG TAKNKFFYMY VQELNYLIRF FTLNSPILHG
ELEEMLKQHT HLFLQHYQSK MNAIKSEKDV KALKNLLYSC KRAV
