ID   ATPE_MICLC              Reviewed;          91 AA.
AC   P80286; C5CA79;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 2.
DT   03-AUG-2022, entry version 110.
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; OrderedLocusNames=Mlut_08190;
OS   Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 /
OS   NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus.
OX   NCBI_TaxID=465515;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC
RC   2665 / VKM Ac-2230;
RX   PubMed=19948807; DOI=10.1128/jb.01254-09;
RA   Young M., Artsatbanov V., Beller H.R., Chandra G., Chater K.F., Dover L.G.,
RA   Goh E.B., Kahan T., Kaprelyants A.S., Kyrpides N., Lapidus A., Lowry S.R.,
RA   Lykidis A., Mahillon J., Markowitz V., Mavromatis K., Mukamolova G.V.,
RA   Oren A., Rokem J.S., Smith M.C., Young D.I., Greenblatt C.L.;
RT   "Genome sequence of the Fleming strain of Micrococcus luteus, a simple
RT   free-living actinobacterium.";
RL   J. Bacteriol. 192:841-860(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-25.
RX   PubMed=8011668; DOI=10.1016/0005-2728(94)90133-3;
RA   Grueber G., Godovac-Zimmermann J., Nawroth T.;
RT   "ATP synthesis and hydrolysis of the ATP-synthase from Micrococcus luteus
RT   regulated by an inhibitor subunit and membrane energization.";
RL   Biochim. Biophys. Acta 1186:43-51(1994).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. {ECO:0000250}.
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; CP001628; ACS30348.1; -; Genomic_DNA.
DR   RefSeq; WP_002857254.1; NZ_WBMF01000002.1.
DR   AlphaFoldDB; P80286; -.
DR   SMR; P80286; -.
DR   STRING; 465515.Mlut_08190; -.
DR   PRIDE; P80286; -.
DR   EnsemblBacteria; ACS30348; ACS30348; Mlut_08190.
DR   GeneID; 67423079; -.
DR   KEGG; mlu:Mlut_08190; -.
DR   eggNOG; COG0355; Bacteria.
DR   HOGENOM; CLU_084338_4_0_11; -.
DR   OMA; AADHFVW; -.
DR   OrthoDB; 1696893at2; -.
DR   Proteomes; UP000000738; Chromosome.
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   InterPro; IPR001469; ATP_synth_F1_dsu/esu.
DR   InterPro; IPR020546; ATP_synth_F1_dsu/esu_N.
DR   InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR   Pfam; PF02823; ATP-synt_DE_N; 1.
DR   SUPFAM; SSF51344; SSF51344; 1.
PE   1: Evidence at protein level;
KW   ATP synthesis; Cell membrane; CF(1); Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8011668"
FT   CHAIN           2..91
FT                   /note="ATP synthase epsilon chain"
FT                   /id="PRO_0000188156"
FT   CONFLICT        13
FT                   /note="R -> Y (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        16
FT                   /note="W -> I (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        21
FT                   /note="S -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        24..25
FT                   /note="SA -> TV (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   91 AA;  9186 MW;  23532F1CFA892573 CRC64;
     MAELNVEIVS EERSIWSGAA SAVSARTVNG EIGILPGHTP MLAVLGDGEV VVRTTDGGTV
     TAQAHGGFFS VDHDRVVIAA TSARLGDAAA A