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ATPE_LACLM
ID   ATPE_LACLM              Reviewed;         141 AA.
AC   Q9RAT9; A2RMI1;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 118.
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};
GN   Name=atpC {ECO:0000255|HAMAP-Rule:MF_00530}; OrderedLocusNames=llmg_1945;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10940012; DOI=10.1128/jb.182.17.4738-4743.2000;
RA   Koebmann B.J., Nilsson D., Kuipers O.P., Jensen P.R.;
RT   "The membrane bound H+-ATPase complex is essential for growth of
RT   Lactococcus lactis.";
RL   J. Bacteriol. 182:4738-4743(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
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:0000255|HAMAP-Rule:MF_00530};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00530}.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00530}.
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DR   EMBL; AF059739; AAF02208.1; -; Genomic_DNA.
DR   EMBL; AM406671; CAL98513.1; -; Genomic_DNA.
DR   RefSeq; WP_011835688.1; NZ_WJVF01000007.1.
DR   AlphaFoldDB; Q9RAT9; -.
DR   SMR; Q9RAT9; -.
DR   STRING; 416870.llmg_1945; -.
DR   EnsemblBacteria; CAL98513; CAL98513; llmg_1945.
DR   KEGG; llm:llmg_1945; -.
DR   eggNOG; COG0355; Bacteria.
DR   HOGENOM; CLU_084338_1_0_9; -.
DR   OMA; MGGFAEI; -.
DR   PhylomeDB; Q9RAT9; -.
DR   BioCyc; LLAC416870:LLMG_RS09730-MON; -.
DR   Proteomes; UP000000364; 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   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   3: Inferred from homology;
KW   ATP synthesis; Cell membrane; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Transport.
FT   CHAIN           1..141
FT                   /note="ATP synthase epsilon chain"
FT                   /id="PRO_0000188148"
SQ   SEQUENCE   141 AA;  15585 MW;  9CE9B55B890CF31A CRC64;
     MSENVMTLQV ITPAGVVYDH HANYITARTT NGEIGILPNM ISTITGLEID ELKVSRPDDE
     THVDYIAVNG GIIEIKDSLV TIVADSAERN RDIDVSRAER AKIRAEKALE VAKAEKKSDE
     IKRVEVALHR ALNRLNVSSH N
 
 
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