ID   VATB_HELVI              Reviewed;         494 AA.
AC   P31410;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=V-type proton ATPase subunit B;
DE            Short=V-ATPase subunit B;
DE   AltName: Full=Vacuolar proton pump subunit B;
GN   Name=VHA55;
OS   Heliothis virescens (Tobacco budworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Heliothis.
OX   NCBI_TaxID=7102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Midgut;
RX   PubMed=1834020; DOI=10.1016/0003-9861(91)90109-v;
RA   Gill S.S., Ross L.S.;
RT   "Molecular cloning and characterization of the B subunit of a vacuolar
RT   H(+)-ATPase from the midgut and Malpighian tubules of Helicoverpa
RT   virescens.";
RL   Arch. Biochem. Biophys. 291:92-99(1991).
CC   -!- FUNCTION: Non-catalytic subunit of the V1 complex of vacuolar(H+)-
CC       ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral
CC       complex (V1) that hydrolyzes ATP and a membrane integral complex (V0)
CC       that translocates protons (By similarity). V-ATPase is responsible for
CC       acidifying and maintaining the pH of intracellular compartments and in
CC       some cell types, is targeted to the plasma membrane, where it is
CC       responsible for acidifying the extracellular environment (By
CC       similarity). Essential for the proper assembly and activity of V-ATPase
CC       (By similarity). {ECO:0000250|UniProtKB:P15313}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC       complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC       V0 complex (By similarity). The V1 complex consists of three catalytic
CC       AB heterodimers that form a heterohexamer, three peripheral stalks each
CC       consisting of EG heterodimers, one central rotor including subunits D
CC       and F, and the regulatory subunits C and H (By similarity). The proton
CC       translocation complex V0 consists of the proton transport subunit a, a
CC       ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f,
CC       and the accessory subunits VhaAC45 and ATP6AP2 (By similarity).
CC       {ECO:0000250|UniProtKB:P21281}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; S61797; AAB20098.1; -; mRNA.
DR   PIR; S18395; S18395.
DR   AlphaFoldDB; P31410; -.
DR   SMR; P31410; -.
DR   GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   ATP-binding; Hydrogen ion transport; Ion transport; Nucleotide-binding;
KW   Transport.
FT   CHAIN           1..494
FT                   /note="V-type proton ATPase subunit B"
FT                   /id="PRO_0000144633"
FT   BINDING         384
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P21281"
SQ   SEQUENCE   494 AA;  54894 MW;  2D20C581D8AE4C76 CRC64;
     MAKTLTASQA AKEHVLAVSR DFISQPRLIY KTVSGVNGPL VILDDVKFPK FSEIVQLRLA
     DGTLRSGQVL EVSGTKAVVQ VFEGTSGIDA KNTLCEFTGD ILRTPVSEDM LGRVFNGSGK
     PIDKGPPILA EDFLDIQGQP INPWSRIYPE EMIQTGISAI DVMNSIARGQ KIPIFSAAGL
     PHNEIAAQIC RQAGLVKIPG KSVLDDHEDN FAIVFAAMGV NMETARFFKQ DFEENGSMEN
     VCLFLNLAND PTIERIITPR LALTAAEFLA YQCEKHVLVI LTDMSSYAEA LREVSAAREE
     VPGRRGFPGY MYTDLATIYE RAGRVEGRNG SITQIPILTM PNDDITHPIP DLTGYITEGQ
     IYVDRQLHNR QIYPPVNVLP SLSRLMKSAI GEGMTRKDHS DVSNQLYACY AIGKDVQAMK
     AVVGEEALTP DDLLYLEFLT KFEKNFISQG NYENRTVFES LDIGWQLLRI FPKEMLKRIP
     ASILAEFYPR DSRH