ID   VATB_CENSY              Reviewed;         462 AA.
AC   A0RXK0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=CENSYa_1445;
OS   Cenarchaeum symbiosum (strain A).
OC   Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX   NCBI_TaxID=414004;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A;
RX   PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA   Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA   Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT   "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT   symbiosum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DP000238; ABK78067.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0RXK0; -.
DR   SMR; A0RXK0; -.
DR   STRING; 414004.CENSYa_1445; -.
DR   EnsemblBacteria; ABK78067; ABK78067; CENSYa_1445.
DR   KEGG; csy:CENSYa_1445; -.
DR   PATRIC; fig|414004.10.peg.1329; -.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; MLMMDSV; -.
DR   Proteomes; UP000000758; 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; 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   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..462
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_0000322499"
SQ   SEQUENCE   462 AA;  50587 MW;  B911A78CE772FD04 CRC64;
     MTVEGGVQYS RIAEIKGPLV IVDGVENAAF DELVEIETNE GGRRLGKVLE IGNGKAIVQV
     FEGTTGLSVA GTNARFVGKV MEMPVSREVL GRIFDGLGRP KDKLPDPIAD KFIDINGEAM
     NPEQREYPKD FIQTGVSAID GIMTLVRGQK LPIFSGSGMS HNILAAQIAR QASVVGTGDD
     FAVVFAAIGV QYSEAEYFRR SLEESGALKR SVLFLNLAND PAIERIITPR VALTVAEYLA
     FDLGMHVLVI LTDMTNYAEA LREISAAREE VPGRKGYPGY LYTDLSTIYE RAGRLVGRKG
     SVTQVPILTM PSDDITHPIP DLTGYITEGQ VVLGRDLFRQ GVYPPVNILM SLSRLMKDGI
     GEGRTREDHQ EISNQNYDAY SRAQEVRALA GIVGKAGLTD IDLRYMGVGD SLEQRLLTQA
     TDENRTIEET LGIMWDTVSG LPKNELTKVK DKYVEKFYKG SA