ID   ATPE_BACSU              Reviewed;         132 AA.
AC   P37812;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 142.
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=BSU36800;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7961438; DOI=10.1128/jb.176.22.6802-6811.1994;
RA   Santana M., Ionescu M.S., Vertes A., Longin R., Kunst F., Danchin A.,
RA   Glaser P.;
RT   "Bacillus subtilis F0F1 ATPase: DNA sequence of the atp operon and
RT   characterization of atp mutants.";
RL   J. Bacteriol. 176:6802-6811(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 89-132.
RC   STRAIN=168;
RA   Glaser P., Danchin A., Kunst F., Moszer I.;
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 1-18.
RC   STRAIN=168 / JH642;
RX   PubMed=8755892; DOI=10.1128/jb.178.15.4611-4619.1996;
RA   Graumann P., Schroeder K., Schmid R., Marahiel M.A.;
RT   "Cold shock stress-induced proteins in Bacillus subtilis.";
RL   J. Bacteriol. 178:4611-4619(1996).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH SPOIIIJ AND YQJG.
RC   STRAIN=168;
RX   PubMed=19717609; DOI=10.1128/jb.00853-09;
RA   Saller M.J., Fusetti F., Driessen A.J.;
RT   "Bacillus subtilis SpoIIIJ and YqjG function in membrane protein
RT   biogenesis.";
RL   J. Bacteriol. 191:6749-6757(2009).
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 (Probable). The F(1)F(0) complex interacts with
CC       SpoIIIJ and YqjG; YqgA is found in the same complex.
CC       {ECO:0000269|PubMed:19717609, ECO:0000305}.
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; Z28592; CAA82261.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15697.1; -; Genomic_DNA.
DR   EMBL; Z81356; CAB03676.1; -; Genomic_DNA.
DR   PIR; I40369; I40369.
DR   RefSeq; NP_391561.1; NC_000964.3.
DR   RefSeq; WP_003227688.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P37812; -.
DR   SMR; P37812; -.
DR   IntAct; P37812; 2.
DR   STRING; 224308.BSU36800; -.
DR   jPOST; P37812; -.
DR   PaxDb; P37812; -.
DR   PRIDE; P37812; -.
DR   EnsemblBacteria; CAB15697; CAB15697; BSU_36800.
DR   GeneID; 936994; -.
DR   KEGG; bsu:BSU36800; -.
DR   PATRIC; fig|224308.179.peg.3986; -.
DR   eggNOG; COG0355; Bacteria.
DR   InParanoid; P37812; -.
DR   OMA; MGGFAEI; -.
DR   PhylomeDB; P37812; -.
DR   BioCyc; BSUB:BSU36800-MON; -.
DR   SABIO-RK; P37812; -.
DR   Proteomes; UP000001570; 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); IBA:GO_Central.
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; -; 1.
DR   HAMAP; MF_00530; ATP_synth_epsil_bac; 1.
DR   InterPro; IPR036794; ATP_F1_dsu/esu_C_sf.
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; SSF46604; SSF46604; 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; Reference proteome;
KW   Transport.
FT   CHAIN           1..132
FT                   /note="ATP synthase epsilon chain"
FT                   /id="PRO_0000188101"
FT   REGION          88..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   132 AA;  14209 MW;  E0FC642847CD63AA CRC64;
     MKTVKVNIVT PDGPVYDADI EMVSVRAESG DLGILPGHIP TVAPLKIGAV RLKKDGQTEM
     VAVSGGFVEV RPDHVTILAQ AAETAEGIDK ERAEAARQRA QERLNSQSDD TDIRRAELAL
     QRALNRLDVA GK