ATPE_BACP3
ID ATPE_BACP3 Reviewed; 132 AA.
AC P07678; Q9KW63;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 118.
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 Bacillus sp. (strain PS3).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-2, AND SUBUNIT.
RX PubMed=2872924; DOI=10.1016/0167-4781(86)90069-2;
RA Saishu T., Nojima H., Kagawa Y.;
RT "Stability of structures of the epsilon subunit and terminator of
RT thermophilic ATPase.";
RL Biochim. Biophys. Acta 867:97-106(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2894854; DOI=10.1016/0005-2728(88)90064-3;
RA Ohta S., Yohda M., Ishizuka M., Hirata H., Hamamoto T.,
RA Otawara-Hamamoto Y., Matsuda K., Kagawa Y.;
RT "Sequence and over-expression of subunits of adenosine triphosphate
RT synthase in thermophilic bacterium PS3.";
RL Biochim. Biophys. Acta 933:141-155(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10958801; DOI=10.1074/jbc.m006575200;
RA Kato-Yamada Y., Yoshida M., Hisabori T.;
RT "Movement of the helical domain of the epsilon subunit is required for the
RT activation of thermophilic F1-ATPase.";
RL J. Biol. Chem. 275:35746-35750(2000).
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. {ECO:0000269|PubMed:2872924}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATPase epsilon chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA96810.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X03969; CAA27607.1; -; Genomic_DNA.
DR EMBL; X07804; CAA30656.1; -; Genomic_DNA.
DR EMBL; AB044942; BAA96810.1; ALT_FRAME; Genomic_DNA.
DR PDB; 2E5Y; X-ray; 1.92 A; A/B=1-132.
DR PDBsum; 2E5Y; -.
DR AlphaFoldDB; P07678; -.
DR BMRB; P07678; -.
DR SMR; P07678; -.
DR TCDB; 3.A.2.1.14; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR PRIDE; P07678; -.
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; 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 3D-structure; ATP synthesis; Cell membrane; CF(1);
KW Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane;
KW Transport.
FT CHAIN 1..132
FT /note="ATP synthase epsilon chain"
FT /id="PRO_0000188097"
FT CONFLICT 74
FT /note="N -> K (in Ref. 3; BAA96810)"
FT /evidence="ECO:0000305"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:2E5Y"
FT STRAND 13..27
FT /evidence="ECO:0007829|PDB:2E5Y"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:2E5Y"
FT STRAND 41..54
FT /evidence="ECO:0007829|PDB:2E5Y"
FT STRAND 57..71
FT /evidence="ECO:0007829|PDB:2E5Y"
FT STRAND 74..84
FT /evidence="ECO:0007829|PDB:2E5Y"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:2E5Y"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:2E5Y"
FT HELIX 112..129
FT /evidence="ECO:0007829|PDB:2E5Y"
SQ SEQUENCE 132 AA; 14334 MW; 372928356D0A0467 CRC64;
MKTIHVSVVT PDGPVYEDDV EMVSVKAKSG ELGILPGHIP LVAPLEISAA RLKKGGKTQY
IAVSGGFLEV RPDNVTILAQ AAERAEDIDV LRAKARKSGR TPLQSQQDDI DFKRAELALK
RAMNRLSVAE MK