ID   ATPE_STRLI              Reviewed;         124 AA.
AC   P0A2Z7; P50011;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 71.
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;
OS   Streptomyces lividans.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-14.
RC   STRAIN=66 / 1326;
RX   PubMed=7828915; DOI=10.1016/0378-1119(95)00673-t;
RA   Hensel M., Lill H., Schmid R., Deckers-Hebestreit G., Altendorf K.;
RT   "The ATP synthase (F1F0) of Streptomyces lividans: sequencing of the atp
RT   operon and phylogenetic considerations with subunit beta.";
RL   Gene 152:11-17(1995).
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: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family. {ECO:0000305}.
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DR   EMBL; Z22606; CAA80328.1; -; Genomic_DNA.
DR   PIR; S37548; S37548.
DR   AlphaFoldDB; P0A2Z7; -.
DR   SMR; P0A2Z7; -.
DR   GO; GO:0005886; C:plasma 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; IPR020546; ATP_synth_F1_dsu/esu_N.
DR   InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR   PANTHER; PTHR13822; PTHR13822; 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   ATP synthesis; Cell membrane; CF(1); Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7828915"
FT   CHAIN           2..124
FT                   /note="ATP synthase epsilon chain"
FT                   /id="PRO_0000188215"
FT   REGION          99..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   124 AA;  13018 MW;  CC69D8FB510C81B7 CRC64;
     MAAELHVALV AADREVWSGE ATLVVARTTS GDIGVMPGHQ PLLGVLESGP VTIRTSDGGT
     VVAAVHGGFI SFADNKLSLL AEVAELSDEI DVHRAERKLE QAKTEGDAHA ERRADVRLRA
     AAGR