ATPE_RHOP5
ID ATPE_RHOP5 Reviewed; 135 AA.
AC Q07UZ6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=RPE_0279;
OS Rhodopseudomonas palustris (strain BisA53).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisA53;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-Rule:MF_00530}.
CC -!- SUBCELLULAR LOCATION: Cell inner 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; CP000463; ABJ04238.1; -; Genomic_DNA.
DR RefSeq; WP_011661732.1; NC_008435.1.
DR AlphaFoldDB; Q07UZ6; -.
DR SMR; Q07UZ6; -.
DR STRING; 316055.RPE_0279; -.
DR EnsemblBacteria; ABJ04238; ABJ04238; RPE_0279.
DR KEGG; rpe:RPE_0279; -.
DR eggNOG; COG0355; Bacteria.
DR HOGENOM; CLU_084338_2_1_5; -.
DR OMA; AWGFVEV; -.
DR OrthoDB; 1696893at2; -.
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; IPR020546; ATP_synth_F1_dsu/esu_N.
DR InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR PANTHER; PTHR13822; PTHR13822; 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 inner membrane; Cell membrane; CF(1);
KW Hydrogen ion transport; Ion transport; Membrane; Transport.
FT CHAIN 1..135
FT /note="ATP synthase epsilon chain"
FT /id="PRO_1000056524"
SQ SEQUENCE 135 AA; 14181 MW; 6EC116C248DCDB69 CRC64;
MATFHFDLVS PEKLAFSGEV DQVDVPGIEG DFGVLANHAP VVAVIRPGIL TVITGGNQQK
IVVLGGIAEV SEKGLTVLAD VATSVADLDA AMFAQTVSSM ESALAGKQGS ELDRAIERLD
HYKNIQHQLT ATAMH