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ATPE_PROMM
ID   ATPE_PROMM              Reviewed;         133 AA.
AC   Q7TUS2;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 107.
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=PMT_1452;
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. {ECO:0000255|HAMAP-Rule:MF_00530}.
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:0000255|HAMAP-
CC       Rule:MF_00530}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       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; BX548175; CAE21627.1; -; Genomic_DNA.
DR   RefSeq; WP_011130820.1; NC_005071.1.
DR   AlphaFoldDB; Q7TUS2; -.
DR   SMR; Q7TUS2; -.
DR   STRING; 74547.PMT_1452; -.
DR   EnsemblBacteria; CAE21627; CAE21627; PMT_1452.
DR   KEGG; pmt:PMT_1452; -.
DR   eggNOG; COG0355; Bacteria.
DR   HOGENOM; CLU_084338_1_2_3; -.
DR   OMA; MGGFAEI; -.
DR   OrthoDB; 1696893at2; -.
DR   Proteomes; UP000001423; Chromosome.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid 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; CF(1); Hydrogen ion transport; Ion transport; Membrane;
KW   Reference proteome; Thylakoid; Transport.
FT   CHAIN           1..133
FT                   /note="ATP synthase epsilon chain"
FT                   /id="PRO_0000188177"
FT   REGION          103..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   133 AA;  14048 MW;  394B94967154E9B2 CRC64;
     MSLTLRVLAP DQSVFDGTAE EVILPSTTGL IGILPGHISL VTALDIGVMR VRANGAWNSI
     ALMGGFAEVE ADDVTVLVNG AELGKSIDAT TAEAELEQAK AKVSQMEGQE PSTEKIKAQQ
     NFNRARARVQ ATK
 
 
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