ID   VATB_TRYCO              Reviewed;         485 AA.
AC   Q26976;
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;
DE            Short=V-ATPase subunit B;
DE   AltName: Full=Vacuolar proton pump subunit B;
OS   Trypanosoma congolense.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas.
OX   NCBI_TaxID=5692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=IL3000;
RA   Fish W.R., Muriuki C.W., Ndegwa D.M., Murphy N.B.;
RL   Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
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; Z25815; CAA81063.1; -; mRNA.
DR   PIR; S37050; S37050.
DR   AlphaFoldDB; Q26976; -.
DR   SMR; Q26976; -.
DR   PRIDE; Q26976; -.
DR   VEuPathDB; TriTrypDB:TcIL3000.11.12320; -.
DR   VEuPathDB; TriTrypDB:TcIL3000.A.H_000979800; -.
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..485
FT                   /note="V-type proton ATPase subunit B"
FT                   /id="PRO_0000144636"
SQ   SEQUENCE   485 AA;  54605 MW;  6AA91D67E69A6A35 CRC64;
     MLSKQELLTE HINELRKDYV VKPRLEYTTI RAVNGPLVIL GDVRLPTFAE IVNIELSDGT
     MRRGQVLEVD GDKAVVQVFE GTSGIDVMRS KCEFTGKVME LGVSEDMLGR VFNGSGIPID
     DGPPVLAEQY RDIQGIPINP RARVYPEEMI QTGISSIDVM TSISRGQKIP LFSGAGLPHN
     EIAAQIVRQA GLVRKEGKQE DFCIVFAAMG VNQETARFFR TEFEENGSME KTVLFMNLAN
     DPTIERIVTP RLALTTAEYL AYDCGKHVLV ILTDMSSYAD ALREVSAARE EVPGRRGFPG
     YMYTDLACIY ERAGRVLGRA GSITQIPILT MPNDDITHPI PDLTGYITEG QIYVDRQLHN
     RQLYPPINIL PSLSRLMKNA IGEGMTRRDH SGVSNQMYAR MRLDDILAMK AVVGEETLSS
     EDLLHLEFLE KFEKKFICQG FHESRDVFQS LDLCWQLLRI FPKVLLNKID VKTRNEFYDG
     QPMRC