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ATPG_LACAC
ID   ATPG_LACAC              Reviewed;         320 AA.
AC   Q9RGY2; Q5FKY1;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=ATP synthase gamma chain {ECO:0000255|HAMAP-Rule:MF_00815};
DE   AltName: Full=ATP synthase F1 sector gamma subunit {ECO:0000255|HAMAP-Rule:MF_00815};
DE   AltName: Full=F-ATPase gamma subunit {ECO:0000255|HAMAP-Rule:MF_00815};
GN   Name=atpG {ECO:0000255|HAMAP-Rule:MF_00815}; OrderedLocusNames=LBA0777;
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. The gamma chain is believed to be important in
CC       regulating ATPase activity and the flow of protons through the CF(0)
CC       complex.
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_00815};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00815}.
CC   -!- INDUCTION: By low pH. {ECO:0000269|PubMed:10510230}.
CC   -!- SIMILARITY: Belongs to the ATPase gamma chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00815}.
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DR   EMBL; AF098522; AAF22497.1; -; Genomic_DNA.
DR   EMBL; CP000033; AAV42643.1; -; Genomic_DNA.
DR   RefSeq; WP_003546744.1; NC_006814.3.
DR   RefSeq; YP_193674.1; NC_006814.3.
DR   AlphaFoldDB; Q9RGY2; -.
DR   SMR; Q9RGY2; -.
DR   STRING; 272621.LBA0777; -.
DR   PRIDE; Q9RGY2; -.
DR   EnsemblBacteria; AAV42643; AAV42643; LBA0777.
DR   GeneID; 56942404; -.
DR   KEGG; lac:LBA0777; -.
DR   PATRIC; fig|272621.13.peg.739; -.
DR   eggNOG; COG0224; Bacteria.
DR   HOGENOM; CLU_050669_0_1_9; -.
DR   OMA; MQITSAM; -.
DR   BioCyc; LACI272621:G1G49-793-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   GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR   CDD; cd12151; F1-ATPase_gamma; 1.
DR   HAMAP; MF_00815; ATP_synth_gamma_bact; 1.
DR   InterPro; IPR035968; ATP_synth_F1_ATPase_gsu.
DR   InterPro; IPR000131; ATP_synth_F1_gsu.
DR   InterPro; IPR023632; ATP_synth_F1_gsu_CS.
DR   PANTHER; PTHR11693; PTHR11693; 1.
DR   Pfam; PF00231; ATP-synt; 1.
DR   PRINTS; PR00126; ATPASEGAMMA.
DR   SUPFAM; SSF52943; SSF52943; 1.
DR   TIGRFAMs; TIGR01146; ATPsyn_F1gamma; 1.
DR   PROSITE; PS00153; ATPASE_GAMMA; 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..320
FT                   /note="ATP synthase gamma chain"
FT                   /id="PRO_0000073298"
SQ   SEQUENCE   320 AA;  35477 MW;  4DA9290ADC9C2457 CRC64;
     MPASLLELKR KIASVKQTGK ITEAMRMVSA SKLNQTENRD KDYTVYNDHV RKTISHLISS
     QVVDSLRERD ISIDKNNISK IDYTDVFGLG ITADMIQPRK NIKTTGFLVV TGDRGLVGSY
     NSSVIKNMMS IFDDERAQGR EVKVLAVGSV GAQFFKKNNV NVVYEKDGVS DVPTFDEVLP
     IVSTAIKMFL NGVYDQLYVC YTHHVNSLSS AFRVEKMLPI VDLDIGVKEA EAHKELEYDI
     EPDVNSVLMK LLPQYARSTI YGAILDAKTA EHASSMTAMQ SATDNANDLV SNLTTKLNRA
     RQAQITTEIT EIISGANALE
 
 
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