ID   VATB_AERPE              Reviewed;         463 AA.
AC   Q9YF36;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=V-type ATP synthase beta chain;
DE   AltName: Full=V-ATPase subunit B;
GN   Name=atpB; OrderedLocusNames=APE_0404.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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       (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; BA000002; BAA79360.2; -; Genomic_DNA.
DR   PIR; D72733; D72733.
DR   AlphaFoldDB; Q9YF36; -.
DR   SMR; Q9YF36; -.
DR   STRING; 272557.APE_0404.1; -.
DR   EnsemblBacteria; BAA79360; BAA79360; APE_0404.1.
DR   KEGG; ape:APE_0404.1; -.
DR   PATRIC; fig|272557.25.peg.301; -.
DR   eggNOG; arCOG00865; Archaea.
DR   Proteomes; UP000002518; 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; 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   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..463
FT                   /note="V-type ATP synthase beta chain"
FT                   /id="PRO_0000144649"
SQ   SEQUENCE   463 AA;  51632 MW;  C4D4AB48926508BD CRC64;
     MALGVREYRN ISEIKGPLLV VEGVSRVAYD EIVEVETAAG EKRRGRVLEV GMGYAVVQVF
     EGTTGISPTG TVVRFMGRPL EIPVTEDMLG RIMNGLGEPI DGGPKIDADE RRDVNGAPLN
     PAERAYPEDF IQTGVSAIDG MNTLVRGQKL PIFSGAGLPH NRLAAQIARQ ATVRGEEEEF
     AVVFSAIGIK YDDFLFFKKF FEETGALGRV AMFVNLADEP AMIRLITPRA ALTLAEYLAY
     ERDMHVLVII TDMTNYAEAL REISAAREEV PGRQGYPGYL YSDLASIYER AGRVKGKKGS
     ITQMPILTMP NDDITHPIPD LTGYITEGQI VLSRELHNRG IYPPINVLMS LSRLMKEGIG
     PGKTREDHAE VSNQLYASYS RGVELRSLTA VVGEESLSER DRRYLKFADL FEQRFLKQGE
     RENRSIEETL DIAWEILSVL PEEELVNIKE ETIKKYHPKY RAG