位置:首页 > 蛋白库 > ATPE_BACP3
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024