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ATPG_MYCGA
ID   ATPG_MYCGA              Reviewed;         289 AA.
AC   P33257;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   15-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 126.
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=MYCGA3050;
GN   ORFNames=MGA_1174;
OS   Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS   (Mycoplasmoides gallisepticum).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=710127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A5969Var.B;
RX   PubMed=1386735; DOI=10.1042/bj2850881;
RA   Rasmussen O.F., Shirvan M.H., Margalit H., Christiansen C., Rottem S.;
RT   "Nucleotide sequence, organization and characterization of the atp genes
RT   and the encoded subunits of Mycoplasma gallisepticum ATPase.";
RL   Biochem. J. 285:881-888(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R(low / passage 15 / clone 2);
RX   PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA   Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA   Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT   "The complete genome sequence of the avian pathogen Mycoplasma
RT   gallisepticum strain R(low).";
RL   Microbiology 149:2307-2316(2003).
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   -!- 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   -!- SIMILARITY: Belongs to the ATPase gamma chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00815}.
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DR   EMBL; X64256; CAA45550.1; -; Genomic_DNA.
DR   EMBL; AE015450; AAP56655.1; -; Genomic_DNA.
DR   PIR; S24338; S24338.
DR   RefSeq; WP_011113546.1; NC_004829.2.
DR   AlphaFoldDB; P33257; -.
DR   SMR; P33257; -.
DR   KEGG; mga:MGA_1174; -.
DR   PATRIC; fig|233150.7.peg.339; -.
DR   HOGENOM; CLU_050669_0_1_14; -.
DR   OMA; MQITSAM; -.
DR   OrthoDB; 1701531at2; -.
DR   Proteomes; UP000001418; 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   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   3: Inferred from homology;
KW   ATP synthesis; Cell membrane; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Reference proteome; Transport.
FT   CHAIN           1..289
FT                   /note="ATP synthase gamma chain"
FT                   /id="PRO_0000073319"
FT   CONFLICT        56
FT                   /note="V -> I (in Ref. 1; CAA45550)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        69
FT                   /note="T -> I (in Ref. 1; CAA45550)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        102
FT                   /note="S -> N (in Ref. 1; CAA45550)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        115
FT                   /note="T -> I (in Ref. 1; CAA45550)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163
FT                   /note="D -> A (in Ref. 1; CAA45550)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        166
FT                   /note="D -> N (in Ref. 1; CAA45550)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        195
FT                   /note="A -> T (in Ref. 1; CAA45550)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   289 AA;  33094 MW;  B42AE682B9D11D51 CRC64;
     MASMQDLKRR MESITVTHKI TKAMKMLSTV KLNRFKATLG KTKEFYQEFY EVIGAVITNY
     NKTKPRTTTP TNQSTKRLWI VINTQLGLCG SYNTNVGKLL VSELAKDDEI ILVGTKLNSF
     LRTRNHEDQI IHTYSINDKN IDFESSYMIG KHVLELHEKN QYDSIDCVYT NYINSLNFEA
     KKIQLIPADP SIFQADTLDR INDKFPKNIS FEPGVDVIIP ALEKQLLQVI LYGCLIESKV
     CEYASRRNAM DTAAKNADDL YNKYKLLYNQ LRQAKITQEI NEIVAGAAK
 
 
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