CTVE_ASPTN
ID CTVE_ASPTN Reviewed; 424 AA.
AC Q0C9L8;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=ATP synthase subunit beta, mitochondrial {ECO:0000303|PubMed:26954888};
DE EC=7.1.2.2 {ECO:0000250|UniProtKB:P00830};
DE AltName: Full=Citreoviridin biosynthesis protein E {ECO:0000305};
DE Flags: Precursor;
GN Name=ctvE {ECO:0000303|PubMed:26954888}; ORFNames=ATEG_09616;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=26954888; DOI=10.1021/acs.orglett.6b00299;
RA Lin T.S., Chiang Y.M., Wang C.C.;
RT "Biosynthetic pathway of the reduced polyketide product citreoviridin in
RT Aspergillus terreus var. aureus revealed by heterologous expression in
RT Aspergillus nidulans.";
RL Org. Lett. 18:1366-1369(2016).
CC -!- FUNCTION: ATP synthase subunit beta; part of the gene cluster that
CC mediates the biosynthesis of citreoviridin, an inhibitor of the of F1-
CC ATPase beta-subunit (PubMed:26954888). Mitochondrial membrane ATP
CC synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in
CC the presence of a proton gradient across the membrane which is
CC generated by electron transport complexes of the respiratory chain (By
CC similarity). Whereas ctvA to ctvD constitute the core biosynthetic gene
CC cluster, ctvE acts as a self-resistance gene (PubMed:26954888).
CC {ECO:0000250|UniProtKB:P00830, ECO:0000305|PubMed:26954888}.
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:0000250|UniProtKB:P00830};
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 (By similarity). {ECO:0000250|UniProtKB:P00830}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00830}. Note=Peripheral membrane protein (By
CC similarity). {ECO:0000250|UniProtKB:P00830}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU29807.1; Type=Erroneous gene model prediction; Evidence={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; CH476608; EAU29807.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001218238.1; XM_001218237.1.
DR AlphaFoldDB; Q0C9L8; -.
DR SMR; Q0C9L8; -.
DR STRING; 341663.Q0C9L8; -.
DR GeneID; 4354472; -.
DR eggNOG; KOG1350; Eukaryota.
DR HOGENOM; CLU_022398_0_2_1; -.
DR OrthoDB; 495235at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
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 InterPro; IPR003593; AAA+_ATPase.
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 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 3: Inferred from homology;
KW ATP synthesis; ATP-binding; CF(1); Hydrogen ion transport; Ion transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW Reference proteome; Transit peptide; Translocase; Transport.
FT TRANSIT 1..60
FT /note="Mitochondrion"
FT CHAIN 61..424
FT /note="ATP synthase subunit beta, mitochondrial"
FT /id="PRO_0000437742"
FT BINDING 187..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00830"
FT BINDING 188..195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00830"
FT BINDING 219..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00830"
FT BINDING 374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00830"
SQ SEQUENCE 424 AA; 45139 MW; C768026E47DE7383 CRC64;
MFRLSSGLLK GGACASRSRI PQLGRSLYST ATSAGADKTQ GKIHTVIGAV VDVQFNHGRL
PPILNALETT NQGKKLVLEV AQHLGEHTVR CIAMDGTEGL VRGTAVADTG NPIMVPVGPA
TLGRIMNVTG DPIDERGPIE GVRLMPIHTE PPAYTEQSTH AEILVTGIKV VDLLAPYARG
GKIGLFGGAG VGKTVFIQEL INNIAKAHGG YSVFTGVGER TREGNDLYHE MQETGVIKLD
GDSKVALVFG QMNEPPGARA RVALTGLTIA EYFRDEGQDV LLFIDNIFRF TQAGSEVSAL
LGRIPSAVGY QPTLAVDMGA MQERITTTTK GSITSVQAVY VPADDLTDPA PATTFIHLDA
TTELSRGISE LGIYPAVDPL GSKSRLMDPR IVGEEHYDTA MRVQRTLQEY KSLQDIIAIL
AGVA
