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VATB_METST
ID   VATB_METST              Reviewed;         467 AA.
AC   Q2NF88;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=V-type ATP synthase beta chain {ECO:0000255|HAMAP-Rule:MF_00310};
DE   AltName: Full=V-ATPase subunit B {ECO:0000255|HAMAP-Rule:MF_00310};
GN   Name=atpB {ECO:0000255|HAMAP-Rule:MF_00310}; OrderedLocusNames=Msp_1134;
OS   Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS   MCB-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX   PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA   Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT   intestinal archaeon is restricted to methanol and H2 for methane formation
RT   and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(2006).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The archaeal beta chain is a regulatory subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_00310}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_00310}.
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DR   EMBL; CP000102; ABC57515.1; -; Genomic_DNA.
DR   RefSeq; WP_011406714.1; NC_007681.1.
DR   AlphaFoldDB; Q2NF88; -.
DR   SMR; Q2NF88; -.
DR   STRING; 339860.Msp_1134; -.
DR   PRIDE; Q2NF88; -.
DR   EnsemblBacteria; ABC57515; ABC57515; Msp_1134.
DR   GeneID; 41325703; -.
DR   KEGG; mst:Msp_1134; -.
DR   eggNOG; arCOG00865; Archaea.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; MLMMDSV; -.
DR   OrthoDB; 8899at2157; -.
DR   Proteomes; UP000001931; Chromosome.
DR   GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro.
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   HAMAP; MF_00310; ATP_synth_B_arch; 1.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR005724; ATPase_A1-cplx_bsu.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR022879; V-ATPase_su_B/beta.
DR   PANTHER; PTHR43389; PTHR43389; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   PIRSF; PIRSF039114; V-ATPsynth_beta/V-ATPase_B; 1.
DR   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01041; ATP_syn_B_arch; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Hydrogen ion transport; Ion transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..467
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_0000322502"
SQ   SEQUENCE   467 AA;  51666 MW;  0A4B0E3FDEC46E3D CRC64;
     MNDVDIKTRE YTTVSEVAGP LMVVQGVEGA AYNEIVEIET PAGENRTGQV LEVKEDIAVV
     QVFEGTSDLN TESTKVRFTG ETAKIGLSTD MLGRIFNGIG KPIDGGPDII PDQELDVNGS
     PMNPSAREFP AEFIQTGIST IDGMNTLVRG QKLPIFSGSG LPHNELAAQI ARQAKVIAED
     SEFAVIFGAM GITHEEANFF MNEFEQTGAL ERVTVFMNLA DDPAIERIMT PKMALTTAEY
     LAFEKGMHVL VILTDITNYC EALREISSAR NEVPGRRGYP GYMYTDLAGM YERAGRINGK
     EGSITQMPIL VMPQDDITHP IPDLTGYITE GQVVLSRELD RTGIYPPVDV LPSLSRLMSG
     GIGEGRTRED HSGVSDQLYA AYAEGRDLRD LTAVVGEEAL TDRDRKFLKF ADEFEDKFIR
     QSKDEDRSIQ ETLDLGWKLL SILPKTELKR VKDQYVEQYL PQSETEE
 
 
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