ID ATPE_ECOL6 Reviewed; 139 AA. AC P0A6E7; P00832; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 115. 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; Synonyms=papG, uncC; OrderedLocusNames=c4657; OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=199310; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CFT073 / ATCC 700928 / UPEC; RX PubMed=12471157; DOI=10.1073/pnas.252529799; RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., RA Donnenberg M.S., Blattner F.R.; RT "Extensive mosaic structure revealed by the complete genome sequence of RT uropathogenic Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient CC across the membrane. {ECO:0000250}. 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 inner membrane {ECO:0000250}; Peripheral CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ATPase epsilon chain family. {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; AE014075; AAN83089.1; -; Genomic_DNA. DR RefSeq; WP_001251965.1; NZ_CP051263.1. DR AlphaFoldDB; P0A6E7; -. DR SMR; P0A6E7; -. DR MINT; P0A6E7; -. DR STRING; 199310.c4657; -. DR GeneID; 83578729; -. DR KEGG; ecc:c4657; -. DR eggNOG; COG0355; Bacteria. DR HOGENOM; CLU_084338_2_0_6; -. DR BioCyc; ECOL199310:C4657-MONOMER; -. DR Proteomes; UP000001410; 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; 1.20.5.440; ATP synthase delta/epsilon subunit, C-terminal domain; 1. DR Gene3D; 2.60.15.10; F0F1 ATP synthase delta/epsilon subunit, N-terminal; 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; IPR020546; ATP_synth_F1_dsu/esu_N. DR InterPro; IPR020547; ATP_synth_F1_esu_C. DR InterPro; IPR036771; ATPsynth_dsu/esu_N. DR NCBIfam; TIGR01216; ATP_synt_epsi; 1. DR PANTHER; PTHR13822; ATP SYNTHASE DELTA/EPSILON CHAIN; 1. DR PANTHER; PTHR13822:SF10; ATP SYNTHASE EPSILON CHAIN, CHLOROPLASTIC; 1. DR Pfam; PF00401; ATP-synt_DE; 1. DR Pfam; PF02823; ATP-synt_DE_N; 1. DR SUPFAM; SSF46604; Epsilon subunit of F1F0-ATP synthase C-terminal domain; 1. DR SUPFAM; SSF51344; Epsilon subunit of F1F0-ATP synthase N-terminal domain; 1. PE 3: Inferred from homology; KW ATP synthesis; Cell inner membrane; Cell membrane; CF(1); KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome; KW Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..139 FT /note="ATP synthase epsilon chain" FT /id="PRO_0000188134" SQ SEQUENCE 139 AA; 15068 MW; 5EFF7DE911745A62 CRC64; MAMTYHLDVV SAEQQMFSGL VEKIQVTGSE GELGIYPGHA PLLTAIKPGM IRIVKQHGHE EFIYLSGGIL EVQPGNVTVL ADTAIRGQDL DEARAMEAKR KAEEHISSSH GDVDYAQASA ELAKAIAQLR VIELTKKAM //