ID   VATB_NITMS              Reviewed;         461 AA.
AC   A9A2Q9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=Nmar_1690;
OS   Nitrosopumilus maritimus (strain SCM1).
OC   Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae;
OC   Nitrosopumilus.
OX   NCBI_TaxID=436308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCM1;
RX   PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA   Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA   Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA   Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA   Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA   Rosenzweig A.C., Manning G., Stahl D.A.;
RT   "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT   nitrification and autotrophy in globally distributed marine crenarchaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
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; CP000866; ABX13586.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9A2Q9; -.
DR   SMR; A9A2Q9; -.
DR   STRING; 436308.Nmar_1690; -.
DR   EnsemblBacteria; ABX13586; ABX13586; Nmar_1690.
DR   KEGG; nmr:Nmar_1690; -.
DR   eggNOG; arCOG00865; Archaea.
DR   HOGENOM; CLU_022916_0_0_2; -.
DR   OMA; MLMMDSV; -.
DR   PhylomeDB; A9A2Q9; -.
DR   Proteomes; UP000000792; Chromosome.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IBA:GO_Central.
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:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
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..461
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_1000115662"
SQ   SEQUENCE   461 AA;  50670 MW;  B5960CB21DED9057 CRC64;
     MTAEGGVQYS KIAEIKGPLV IVDDVENAAF DELVEVETKD GERRLGKVLE VGNGKAIVQV
     FEGTTGLSIA ATNAKFVGKV MEMPVSREVL GRVFDGLGRP KDGLPDPIAD QFIDINGEPM
     NPEQREYPKD FIQTGVSVID GMITLVRGQK LPIFSGSGMS HNLLAAQIAR QASVIGTQDD
     FAVVFAAIGV QYSEAEYFRR SLEESGALKR SVLFLNTADD PAIERIITPR VALTVAEYLA
     FELGMHVLVI LTDMTNYAEA LREISAAREE VPGRKGYPGY LYTDLSTIYE RAGKLNGKKG
     SVTQVPILSM PSDDITHPIP DLTGYITEGQ IVLGRDLFRQ GVYPPVNILM SLSRLMKDGI
     GEGSTRADHG EISNQVYDAY SRAQEVRALA GIVGKAGLTE IDLKYMDVGD VFENEFLSQA
     TDENRTIEET LGILWKIVSK LPRNEITKIK DKYVDQYYKE E