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ATPE_LACAC
ID   ATPE_LACAC              Reviewed;         146 AA.
AC   Q9RGY0; Q5FKX9;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=LBA0779;
OS   Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=272621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], ACTIVITY REGULATION, INDUCTION, AND
RP   PROBABLE OPERON.
RC   STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX   PubMed=10510230; DOI=10.1046/j.1365-2958.1999.01557.x;
RA   Kullen M.J., Klaenhammer T.R.;
RT   "Identification of the pH-inducible, proton-translocating F1F0-ATPase
RT   (atpBEFHAGDC) operon of Lactobacillus acidophilus by differential display:
RT   gene structure, cloning and characterization.";
RL   Mol. Microbiol. 33:1152-1161(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX   PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA   Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA   McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA   Hamrick A., Cano R., Klaenhammer T.R.;
RT   "Complete genome sequence of the probiotic lactic acid bacterium
RT   Lactobacillus acidophilus NCFM.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane.
CC   -!- ACTIVITY REGULATION: Increases 2-fold following exposure to low pH.
CC       {ECO:0000269|PubMed:10510230}.
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   -!- INDUCTION: By low pH. {ECO:0000269|PubMed:10510230}.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00530}.
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DR   EMBL; AF098522; AAF22499.1; -; Genomic_DNA.
DR   EMBL; CP000033; AAV42645.1; -; Genomic_DNA.
DR   RefSeq; WP_003546746.1; NC_006814.3.
DR   RefSeq; YP_193676.1; NC_006814.3.
DR   AlphaFoldDB; Q9RGY0; -.
DR   SMR; Q9RGY0; -.
DR   STRING; 272621.LBA0779; -.
DR   PRIDE; Q9RGY0; -.
DR   EnsemblBacteria; AAV42645; AAV42645; LBA0779.
DR   GeneID; 56942406; -.
DR   KEGG; lac:LBA0779; -.
DR   PATRIC; fig|272621.13.peg.741; -.
DR   eggNOG; COG0355; Bacteria.
DR   HOGENOM; CLU_084338_1_0_9; -.
DR   OMA; MGGFAEI; -.
DR   BioCyc; LACI272621:G1G49-795-MON; -.
DR   Proteomes; UP000006381; 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   2: Evidence at transcript level;
KW   ATP synthesis; Cell membrane; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Reference proteome; Transport.
FT   CHAIN           1..146
FT                   /note="ATP synthase epsilon chain"
FT                   /id="PRO_0000188146"
SQ   SEQUENCE   146 AA;  16473 MW;  C065FFDE3A544D09 CRC64;
     MADPEKLFKV IVVTPNGMIY SHRGSIVDVR AIDGERSILY NHIPILTPLA ISEVKVKRSR
     EMGSRIDHIA ISGGYIEFSN NVATIVADSA ERARNIDVSR AQAAKERAEK RLREAREKHD
     ERNLERAQVA LKRAMNRISV YNARGH
 
 
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