ID   VATB1_ACEAT             Reviewed;         492 AA.
AC   Q38681;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=V-type proton ATPase subunit B 1;
DE            Short=V-ATPase subunit B 1;
DE   AltName: Full=Vacuolar proton pump subunit B 1;
OS   Acetabularia acetabulum (Mermaid's wine glass) (Acetabularia mediterranea).
OC   Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; TCBD clade;
OC   Dasycladales; Polyphysaceae; Acetabularia.
OX   NCBI_TaxID=35845;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ikeda M., Konishi K., Moritani C., Kadowaki H., Rahman H., Ohmori S.;
RT   "Molecular cloning of cDNAs encoding Acetabularia acetabulum V type ATPase,
RT   B subunit.";
RL   (er) Plant Gene Register PGR95-043(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ikeda M., Konishi K., Kadowaki H., Moritani C., Watanabe Y.;
RT   "Molecular cloning of cDNAs encoding Acetabularia acetabulum V type ATPase,
RT   A and B subunits.";
RL   (er) Plant Gene Register PGR96-030(1996).
CC   -!- FUNCTION: Non-catalytic subunit of the peripheral V1 complex of
CC       vacuolar ATPase. V-ATPase is responsible for acidifying a variety of
CC       intracellular compartments in eukaryotic cells.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC       catalytic V1 complex (main components: subunits A, B, C, D, E, and F)
CC       attached to an integral membrane V0 proton pore complex (main
CC       component: the proteolipid protein).
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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; D50530; BAA09099.1; -; mRNA.
DR   AlphaFoldDB; Q38681; -.
DR   SMR; Q38681; -.
DR   PRIDE; Q38681; -.
DR   GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
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; IPR005723; ATPase_V1-cplx_bsu.
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; TIGR01040; V-ATPase_V1_B; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   2: Evidence at transcript level;
KW   Hydrogen ion transport; Ion transport; Transport.
FT   CHAIN           1..492
FT                   /note="V-type proton ATPase subunit B 1"
FT                   /id="PRO_0000144637"
SQ   SEQUENCE   492 AA;  54661 MW;  1D5B96FC1BEED21E CRC64;
     MASADVFKAN VEAVTRDYIC EPRIEYRTVG GVSGPLVVVE LVKRPKFAEI VNIRLGNGTS
     RRGQVLEVDG NRAVVQVFEG TSGIDNRNTT LQFTGEVLST PVSKDMLGRV FNGSGKPIDG
     GPPVLAEAYL DIQGSSINPS ERTYPEEMIQ TGVSTIDVMN SIARGQKIPL FSAAGLPHND
     IAAQICRQAG LVKRGNQDSM IDAGHEEEEF AIVFAAMGVN METAHYFKQD FEENGSMEKT
     VLFLNLANDP TIERIITPRI ALTTAEYLAY ECGKHVLVIL TDMSSYADAL REVSAAREEV
     PGRRGYPGYM YTDLATIYER AGRIEGRKGS ITQLPILTMP NDDITHPIPD LTGYITEGQI
     YVDRQLHNRQ IYPPINVLPS LSRLMKSAIG EGMTRKDHSE VSNQLYANYA IGKDVAAMKA
     VVGEEALSSE DLLYLEFLDK FERKFVNQGH YEARTIFDSL DLAWTLLRLF PKELLRRITA
     KTLEKMYERS ES