ATPG_TRYBB
ID ATPG_TRYBB Reviewed; 305 AA.
AC A0A161CFW5; A0A2U3T1L4;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 1.
DT 25-MAY-2022, entry version 20.
DE RecName: Full=ATP synthase subunit gamma, mitochondrial;
DE AltName: Full=ATP synthase F1 subunit gamma {ECO:0000303|PubMed:19436713};
DE AltName: Full=F(1)F(o)-ATPase gamma subunit {ECO:0000303|PubMed:27518185};
GN Name=ATPF1G {ECO:0000312|EMBL:AOF47129.1};
GN ORFNames=Tb427.10.180 {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:ALK02525.1};
RN [1] {ECO:0000312|EMBL:AOF47129.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF
RP 284-SER--LYS-305.
RC STRAIN=427 {ECO:0000312|EMBL:AOF47129.1};
RX PubMed=27518185; DOI=10.1371/journal.pntd.0004791;
RA Eze A.A., Gould M.K., Munday J.C., Tagoe D.N., Stelmanis V., Schnaufer A.,
RA De Koning H.P.;
RT "Reduced mitochondrial membrane potential is a late adaptation of
RT Trypanosoma brucei brucei to isometamidium preceded by mutations in the
RT gamma subunit of the F1Fo-ATPase.";
RL PLoS Negl. Trop. Dis. 10:E0004791-E0004791(2016).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS),
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
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] {ECO:0000312|EMBL:ALK02525.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=427;
RA Birhanu H.A., Tadesse G., Goddeeris B.M., Van Reet N., Buscher P.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP FUNCTION, PROTEIN SEQUENCE OF 2-6, SUBCELLULAR LOCATION, SUBUNIT, AND
RP 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 -!- 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:19436713, ECO:0000269|PubMed:29247468,
CC ECO:0000269|PubMed:29440423}; Peripheral membrane protein
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 gamma chain family. {ECO:0000305}.
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DR EMBL; KX444506; AOF47129.1; -; Genomic_DNA.
DR EMBL; KT934838; ALK02525.1; -; Genomic_DNA.
DR EMBL; LS423645; SPS16791.1; -; Genomic_DNA.
DR PDB; 6F5D; X-ray; 3.20 A; G=2-305.
DR PDBsum; 6F5D; -.
DR AlphaFoldDB; A0A161CFW5; -.
DR SMR; A0A161CFW5; -.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR CDD; cd12151; F1-ATPase_gamma; 1.
DR InterPro; IPR035968; ATP_synth_F1_ATPase_gsu.
DR InterPro; IPR000131; ATP_synth_F1_gsu.
DR PANTHER; PTHR11693; PTHR11693; 1.
DR Pfam; PF00231; ATP-synt; 1.
DR PRINTS; PR00126; ATPASEGAMMA.
DR SUPFAM; SSF52943; SSF52943; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; CF(1); Direct protein sequencing;
KW Hydrogen ion transport; Hydrolase; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:29247468"
FT CHAIN 2..305
FT /note="ATP synthase subunit gamma, mitochondrial"
FT /id="PRO_0000444143"
FT MUTAGEN 284..305
FT /note="Missing: Confers resistance to killing by ethidium
FT bromide and isometamidium. Decreases mitochondrial membrane
FT potential, and increases time required to reach lethal
FT levels of parasitemia in vivo. Loss of the kinetoplast, a
FT specialized mitochondrial structure that harbors the
FT mitochondrial genome."
FT /evidence="ECO:0000269|PubMed:27518185"
SQ SEQUENCE 305 AA; 34400 MW; 357B2AC8B178B1B9 CRC64;
MSGKLRLYKE KLEGYNRFYS IVKTIKMVTL AKYRAAQGRI RTRDFSLRYT ELAFSKPQAS
RDAVAAAKNA LVYIPITTNR GSCGALNSNI VRCIDSVVSS KMVLMPVGKR GIDSFSKLYP
DEFRYGIIND MKESMHFGYA TFVIENAYEV SKDADRYQVI FNRFVSAGVQ RNAVYNIPSY
EKWKEDLADA ASSDNQKNRY LFANALQNEE EQLIRDFFDF HAALAVLNAV GENELSEQAA
RLVAVEGQLT NISSLQQRTS SLYNKTRQFG ITAALIEILS AMSSLEGNAM KGVRRNKFWE
GAVTK
