ATPE_RICCN
ID ATPE_RICCN Reviewed; 112 AA.
AC Q92G89;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 105.
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; OrderedLocusNames=RC1234;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(2001).
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}.
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DR EMBL; AE006914; AAL03772.1; -; Genomic_DNA.
DR PIR; B97854; B97854.
DR RefSeq; WP_010977799.1; NC_003103.1.
DR AlphaFoldDB; Q92G89; -.
DR SMR; Q92G89; -.
DR EnsemblBacteria; AAL03772; AAL03772; RC1234.
DR KEGG; rco:RC1234; -.
DR PATRIC; fig|272944.4.peg.1415; -.
DR HOGENOM; CLU_084338_2_1_5; -.
DR OMA; QAKMVTM; -.
DR Proteomes; UP000000816; 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; 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..112
FT /note="ATP synthase epsilon chain"
FT /id="PRO_0000188192"
SQ SEQUENCE 112 AA; 12145 MW; B46B44039BBECBBE CRC64;
MNATILVKII TPLSIALEKQ AKMVTMSGEE GMFGVLPSHV PMIVSLKAGL VQVYIDDMHK
SENTYLISGG VTEVTANYIN IATETAINVT NLSEVEIATK LLDLQKTLSD QH