ID   ATPE_SYNY3              Reviewed;         136 AA.
AC   P26533;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   04-NOV-2026, entry version 161.
DE   RecName: Full=ATP synthase epsilon chain;
DE   AltName: Full=ATP synthase F1 sector epsilon subunit;
DE   AltName: Full=F-ATPase epsilon subunit;
GN   Name=atpC; Synonyms=atpE; OrderedLocusNames=slr1330;
OS   Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Merismopediaceae; Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1832989; DOI=10.1007/bf00037050;
RA   Lill H., Nelson N.;
RT   "The atp1 and atp2 operons of the cyanobacterium Synechocystis sp. PCC
RT   6803.";
RL   Plant Mol. Biol. 17:641-652(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-21.
RX   PubMed=9298645; DOI=10.1002/elps.1150180806;
RA   Sazuka T., Ohara O.;
RT   "Towards a proteome project of cyanobacterium Synechocystis sp. strain
RT   PCC6803: linking 130 protein spots with their respective genes.";
RL   Electrophoresis 18:1252-1258(1997).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane.
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.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA18088.1; Type=Erroneous initiation; 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; X58129; CAA41138.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA18088.1; ALT_INIT; Genomic_DNA.
DR   PIR; S75527; S75527.
DR   AlphaFoldDB; P26533; -.
DR   SMR; P26533; -.
DR   FunCoup; P26533; 435.
DR   IntAct; P26533; 7.
DR   STRING; 1148.gene:10498959; -.
DR   PaxDb; 1148-gene:10498959; -.
DR   EnsemblBacteria; BAA18088; BAA18088; BAA18088.
DR   KEGG; syn:slr1330; -.
DR   eggNOG; COG0355; Bacteria.
DR   InParanoid; P26533; -.
DR   OMA; ADHMPLV; -.
DR   PhylomeDB; P26533; -.
DR   BRENDA; 7.1.2.2; 6192.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045259; C:proton-transporting ATP synthase complex; IDA:UniProtKB.
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   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR   CDD; cd12152; F1-ATPase_delta; 1.
DR   Gene3D; 2.60.15.10; F0F1 ATP synthase delta/epsilon subunit, N-terminal; 1.
DR   Gene3D; 1.10.287.540; Helix hairpin bin; 1.
DR   HAMAP; MF_00530; ATP_synth_epsil_bac; 1.
DR   InterPro; IPR001469; ATP_synth_F1_dsu/esu.
DR   InterPro; IPR020546; ATP_synth_F1_dsu/esu_N.
DR   InterPro; IPR020547; ATP_synth_F1_esu_C.
DR   InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR   NCBIfam; TIGR01216; ATP_synt_epsi; 1.
DR   PANTHER; PTHR13822; ATP SYNTHASE DELTA/EPSILON CHAIN; 1.
DR   PANTHER; PTHR13822:SF10; ATP SYNTHASE EPSILON CHAIN, CHLOROPLASTIC; 1.
DR   Pfam; PF00401; ATP-synt_DE; 1.
DR   Pfam; PF02823; ATP-synt_DE_N; 1.
DR   SUPFAM; SSF51344; Epsilon subunit of F1F0-ATP synthase N-terminal domain; 1.
PE   1: Evidence at protein level;
KW   ATP synthesis; CF(1); Direct protein sequencing; Hydrogen ion transport;
KW   Ion transport; Membrane; Reference proteome; Thylakoid; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9298645"
FT   CHAIN           2..136
FT                   /note="ATP synthase epsilon chain"
FT                   /id="PRO_0000188230"
FT   REGION          100..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   136 AA;  14581 MW;  55B8F3545DC23E72 CRC64;
     MTLTVRVITP DKVVWDEEVQ ELILPSTTGQ LGILSNHAPL LTALEIGVMR VRPGKDWQNI
     AVMGGFAEVE NNEVKVLVNG AELGTTIDAE SARQAYTAAQ GALEEANRGE DKPNQLKASN
     NYKKARARLQ AAGGAV
//