ATPE_STAES
ID ATPE_STAES Reviewed; 134 AA.
AC Q8CNJ8;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 112.
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=SE_1699;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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 membrane {ECO:0000255|HAMAP-Rule:MF_00530};
CC Peripheral membrane protein {ECO:0000255|HAMAP-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; AE015929; AAO05298.1; -; Genomic_DNA.
DR RefSeq; NP_765254.1; NC_004461.1.
DR RefSeq; WP_002447782.1; NZ_WBME01000021.1.
DR AlphaFoldDB; Q8CNJ8; -.
DR SMR; Q8CNJ8; -.
DR STRING; 176280.SE_1699; -.
DR EnsemblBacteria; AAO05298; AAO05298; SE_1699.
DR GeneID; 50018200; -.
DR KEGG; sep:SE_1699; -.
DR PATRIC; fig|176280.10.peg.1660; -.
DR eggNOG; COG0355; Bacteria.
DR HOGENOM; CLU_084338_1_3_9; -.
DR OMA; MGGFAEI; -.
DR Proteomes; UP000001411; 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; 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 membrane; CF(1); Hydrogen ion transport; Ion transport;
KW Membrane; Transport.
FT CHAIN 1..134
FT /note="ATP synthase epsilon chain"
FT /id="PRO_0000188206"
FT REGION 94..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 134 AA; 14909 MW; FBC1D55C2F82C702 CRC64;
MNTLRLNIVT PNGSVYERED VEMAVLQTTA GEMGIMYGHI PTVAALKTGH VKVNFHNGNE
FIAVSDGFIE ARQHQLSIIV QTAEPASEID VERAKLAKSR AESHLEDDDD NTDINRAKRA
LERANNRLRV AELQ
