ID   VATB_MANSE              Reviewed;         494 AA.
AC   P31401;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 103.
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   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Midgut;
RX   PubMed=1387326; DOI=10.1016/0167-4781(92)90053-3;
RA   Novak F.J., Graf R., Waring R.B., Wolfersberger M.G., Wieczorek H.,
RA   Harvey W.R.;
RT   "Primary structure of V-ATPase subunit B from Manduca sexta midgut.";
RL   Biochim. Biophys. Acta 1132:67-71(1992).
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; X64354; CAA45706.1; -; mRNA.
DR   PIR; S24387; S24387.
DR   AlphaFoldDB; P31401; -.
DR   SMR; P31401; -.
DR   DIP; DIP-61387N; -.
DR   IntAct; P31401; 1.
DR   BindingDB; P31401; -.
DR   ChEMBL; CHEMBL1781869; -.
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_0000144634"
FT   BINDING         384
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P21281"
SQ   SEQUENCE   494 AA;  54905 MW;  8A8A3A2C04A9CFD6 CRC64;
     MAKTLSAAQA NKEHVLAVSR DFISQPRLTY KTVSGVNGPL VILDEVKFPK FSEIVQLKLA
     DGTHRSGQVL EVSGSKAVVQ 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 KFEKNFITQG NYENRTVFES LDIGWQLLRI FPKEMLKRIP
     ASILAEFYPR DSRH