ATPE_STRP2
ID ATPE_STRP2 Reviewed; 139 AA.
AC Q04N64;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=SPD_1334;
OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=373153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D39 / NCTC 7466;
RX PubMed=17041037; DOI=10.1128/jb.01148-06;
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT pneumoniae and comparison with that of unencapsulated laboratory strain
RT R6.";
RL J. Bacteriol. 189:38-51(2007).
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 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; CP000410; ABJ54693.1; -; Genomic_DNA.
DR RefSeq; WP_000068050.1; NC_008533.2.
DR AlphaFoldDB; Q04N64; -.
DR SMR; Q04N64; -.
DR STRING; 373153.SPD_1334; -.
DR EnsemblBacteria; ABJ54693; ABJ54693; SPD_1334.
DR GeneID; 60233555; -.
DR GeneID; 66806597; -.
DR KEGG; spd:SPD_1334; -.
DR eggNOG; COG0355; Bacteria.
DR HOGENOM; CLU_084338_1_0_9; -.
DR OMA; MGGFAEI; -.
DR OrthoDB; 1696893at2; -.
DR BioCyc; SPNE373153:G1G6V-1439-MON; -.
DR Proteomes; UP000001452; 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; 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; 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..139
FT /note="ATP synthase epsilon chain"
FT /id="PRO_1000056540"
SQ SEQUENCE 139 AA; 15638 MW; 972D40440D879172 CRC64;
MAQLTVQIVT PDGLVYDHHA SYVSVRTLDG EMGILPRHEN MIAVLAVDEV KVKRIDDKDH
VNWIAVNGGV IEIANDMITI VADSAERARD IDISRAERAK LRAERAIEEA QDKHLIDQER
RAKIALQRAI NRINVGNRL