ATPE_DESVM
ID ATPE_DESVM Reviewed; 134 AA.
AC Q9S5B5; B8DRD3;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=DvMF_2832;
OS Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=883;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10735863; DOI=10.1128/jb.182.8.2200-2206.2000;
RA Ozawa K., Meikari T., Motohashi K., Yoshida M., Akutsu H.;
RT "Evidence for the presence of an F-type ATP synthase involved in sulfate
RT respiration in Desulfovibrio vulgaris.";
RL J. Bacteriol. 182:2200-2206(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19637 / Miyazaki F;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C.,
RA Richardson P.;
RT "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL Submitted (OCT-2008) 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.
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; AB022018; BAA83614.1; -; Genomic_DNA.
DR EMBL; CP001197; ACL09770.1; -; Genomic_DNA.
DR RefSeq; WP_015946454.1; NC_011769.1.
DR AlphaFoldDB; Q9S5B5; -.
DR SMR; Q9S5B5; -.
DR STRING; 883.DvMF_2832; -.
DR PRIDE; Q9S5B5; -.
DR EnsemblBacteria; ACL09770; ACL09770; DvMF_2832.
DR KEGG; dvm:DvMF_2832; -.
DR eggNOG; COG0355; Bacteria.
DR HOGENOM; CLU_084338_1_3_7; -.
DR OMA; MGGFAEI; -.
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; 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 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..134
FT /note="ATP synthase epsilon chain"
FT /id="PRO_0000188131"
SQ SEQUENCE 134 AA; 14769 MW; 0C4244380E2771CE CRC64;
MEKSLHLEIV TPDRLVLSEK VDYVGAPGYE GEFGILPNHI PFLSALNIGS LYYKAGGKTH
WIFVSGGFAE VSDNKVTVLA ESAERAEDID LERARKAKER AEQRLAQAKE KLDSARAQAA
LQRAMARMRV RGAA
