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VATB_METTP
ID   VATB_METTP              Reviewed;         463 AA.
AC   A0B9K1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=Mthe_1608;
OS   Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS   PT) (Methanosaeta thermophila).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanotrichales; Methanotrichaceae; Methanothrix.
OX   NCBI_TaxID=349307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT   "Complete sequence of Methanosaeta thermophila PT.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000477; ABK15375.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0B9K1; -.
DR   SMR; A0B9K1; -.
DR   STRING; 349307.Mthe_1608; -.
DR   PRIDE; A0B9K1; -.
DR   EnsemblBacteria; ABK15375; ABK15375; Mthe_1608.
DR   KEGG; mtp:Mthe_1608; -.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; GFKIKPR; -.
DR   Proteomes; UP000000674; Chromosome.
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; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
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; SSF52540; SSF52540; 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..463
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_1000059383"
SQ   SEQUENCE   463 AA;  51084 MW;  0B6BCABD88BAAEB0 CRC64;
     MTKEYKTITE ISGPLVFVEK TEPVGYGELV EIRTASGEVK RGQVLDTSDE IVVVQVFEGT
     GGLSKDSSVR FTGDVIKMPL SPSIIGRVLS GSGRPRDGGP PIVPEVEREI IGAAINPASR
     EKPRAFIQTG ISTIDGTNTL VRGQKLPIFS GAGLPHNDVA LQIARQAKVL GEAEEFAVVF
     CAMGITNEEA QHFMADFERT GALERAVIFL NLADDPAVER LLTPKLGLTT AEYLAFDLDM
     HVLVIYTDMT NYCESLRQMG AAREEVPGRR GYPGYMYTDL ATNYERAGII KGKKGSITQF
     PILTMPGDDI THPIPDLSGY ITEGQLIVSR ELHRKGIYPP IDIRPSLSRL MNSGIGAGHT
     REDHRAVSDQ LYAYYAEGCD LRGLAAIVGK EALSERDKLI LEFADQFERR FVNQGRDEDR
     SIIETLTIGW ELLSMLPETM LTRIDDKFIK KYHPKYAGTA KKE
 
 
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