ATPE_THEVB
ID ATPE_THEVB Reviewed; 138 AA.
AC Q8DLG7;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=ATP synthase epsilon chain {ECO:0000255|HAMAP-Rule:MF_00530};
DE AltName: Full=ATP synthase F1 sector epsilon subunit {ECO:0000255|HAMAP-Rule:MF_00530};
DE AltName: Full=F-ATPase epsilon subunit {ECO:0000255|HAMAP-Rule:MF_00530};
DE Contains:
DE RecName: Full=ATP synthase epsilon chain, N-terminally processed;
GN Name=atpC {ECO:0000255|HAMAP-Rule:MF_00530}; Synonyms=atpE;
GN OrderedLocusNames=tlr0526;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [2]
RP FUNCTION, MASS SPECTROMETRY, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=18206981; DOI=10.1016/j.bbamem.2007.12.017;
RA Suhai T., Dencher N.A., Poetsch A., Seelert H.;
RT "Remarkable stability of the proton translocating F1FO-ATP synthase from
RT the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1.";
RL Biochim. Biophys. Acta 1778:1131-1140(2008).
RN [3]
RP SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=20558739; DOI=10.1074/jbc.m110.127589;
RA Broser M., Gabdulkhakov A., Kern J., Guskov A., Muh F., Saenger W.,
RA Zouni A.;
RT "Crystal structure of monomeric photosystem II from Thermosynechococcus
RT elongatus at 3.6 A resolution.";
RL J. Biol. Chem. 285:26255-26262(2010).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. {ECO:0000269|PubMed:18206981}.
CC -!- FUNCTION: The complex from the organism is particularly stable to
CC disruption and remains functional after 6 hours at 55 degrees Celsius.
CC {ECO:0000269|PubMed:18206981}.
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 four main
CC subunits: a(1), b(1), b'(1) and c(9-12). {ECO:0000269|PubMed:18206981,
CC ECO:0000269|PubMed:20558739}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_00530, ECO:0000269|PubMed:18206981,
CC ECO:0000269|PubMed:20558739}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00530, ECO:0000269|PubMed:18206981}.
CC -!- MASS SPECTROMETRY: [ATP synthase epsilon chain]: Mass=14741;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:18206981};
CC -!- MASS SPECTROMETRY: [ATP synthase epsilon chain, N-terminally
CC processed]: Mass=14619; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:20558739};
CC -!- SIMILARITY: Belongs to the ATPase epsilon chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00530}.
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; BA000039; BAC08078.1; -; Genomic_DNA.
DR RefSeq; NP_681316.1; NC_004113.1.
DR RefSeq; WP_011056376.1; NC_004113.1.
DR PDB; 2RQ6; NMR; -; A=1-138.
DR PDB; 2RQ7; NMR; -; A=1-88.
DR PDB; 5ZWL; X-ray; 1.98 A; E=1-138.
DR PDBsum; 2RQ6; -.
DR PDBsum; 2RQ7; -.
DR PDBsum; 5ZWL; -.
DR AlphaFoldDB; Q8DLG7; -.
DR SMR; Q8DLG7; -.
DR STRING; 197221.22294247; -.
DR EnsemblBacteria; BAC08078; BAC08078; BAC08078.
DR KEGG; tel:tlr0526; -.
DR PATRIC; fig|197221.4.peg.554; -.
DR eggNOG; COG0355; Bacteria.
DR OMA; MGGFAEI; -.
DR OrthoDB; 1696893at2; -.
DR EvolutionaryTrace; Q8DLG7; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid 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-UniRule.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR CDD; cd12152; F1-ATPase_delta; 1.
DR Gene3D; 2.60.15.10; -; 1.
DR HAMAP; MF_00530; ATP_synth_epsil_bac; 1.
DR InterPro; IPR001469; ATP_synth_F1_dsu/esu.
DR InterPro; IPR020547; ATP_synth_F1_dsu/esu_C.
DR InterPro; IPR020546; ATP_synth_F1_dsu/esu_N.
DR InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR PANTHER; PTHR13822; PTHR13822; 1.
DR Pfam; PF00401; ATP-synt_DE; 1.
DR Pfam; PF02823; ATP-synt_DE_N; 1.
DR SUPFAM; SSF51344; SSF51344; 1.
DR TIGRFAMs; TIGR01216; ATP_synt_epsi; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; CF(1); Hydrogen ion transport; Ion transport;
KW Membrane; Reference proteome; Thylakoid; Transport.
FT CHAIN 1..138
FT /note="ATP synthase epsilon chain"
FT /id="PRO_0000188225"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:18206981,
FT ECO:0000269|PubMed:20558739"
FT CHAIN 2..138
FT /note="ATP synthase epsilon chain, N-terminally processed"
FT /id="PRO_0000430772"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:5ZWL"
FT STRAND 10..26
FT /evidence="ECO:0007829|PDB:5ZWL"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:5ZWL"
FT STRAND 40..70
FT /evidence="ECO:0007829|PDB:5ZWL"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:5ZWL"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:5ZWL"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:5ZWL"
FT HELIX 89..108
FT /evidence="ECO:0007829|PDB:5ZWL"
FT HELIX 112..133
FT /evidence="ECO:0007829|PDB:5ZWL"
SQ SEQUENCE 138 AA; 14750 MW; 7C2E1B85283C4E22 CRC64;
MVMTVRVIAP DKTVWDAPAE EVILPSTTGQ LGILSNHAPL LTALETGVMR VRQDREWVAI
ALMGGFAEVE NNEVTILVNG AERGDTIDLE KAKAEFAAAQ AALAQAEQGE SKQAKIQATQ
AFRRARARLQ AAGGVVEI
