ID B3SAY3_TRIAD Unreviewed; 496 AA.
AC B3SAY3;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Vacuolar proton pump subunit B {ECO:0000256|RuleBase:RU366021};
DE Short=V-ATPase subunit B {ECO:0000256|RuleBase:RU366021};
DE AltName: Full=Vacuolar proton pump subunit B {ECO:0000256|RuleBase:RU366021};
GN ORFNames=TRIADDRAFT_32492 {ECO:0000313|EMBL:EDV20070.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV20070.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV20070.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV20070.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
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. V-ATPase is responsible for acidifying and
CC maintaining the pH of intracellular compartments and in some cell
CC types, is targeted to the plasma membrane, where it is responsible for
CC acidifying the extracellular environment.
CC {ECO:0000256|RuleBase:RU366021}.
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. The V1 complex consists of three catalytic AB heterodimers
CC that form a heterohexamer, three peripheral stalks each consisting of
CC EG heterodimers, one central rotor including subunits D and F, and the
CC regulatory subunits C and H. The proton translocation complex V0
CC consists of the proton transport subunit a, a ring of proteolipid
CC subunits c9c'', rotary subunit d, subunits e and f, and the accessory
CC subunits. {ECO:0000256|RuleBase:RU366021}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|RuleBase:RU366021}.
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DR EMBL; DS985263; EDV20070.1; -; Genomic_DNA.
DR RefSeq; XP_002117454.1; XM_002117418.1.
DR AlphaFoldDB; B3SAY3; -.
DR STRING; 10228.B3SAY3; -.
DR EnsemblMetazoa; TriadT32492; TriadP32492; TriadG32492.
DR GeneID; 6758608; -.
DR KEGG; tad:TRIADDRAFT_32492; -.
DR CTD; 6758608; -.
DR eggNOG; KOG1351; Eukaryota.
DR HOGENOM; CLU_022916_3_0_1; -.
DR InParanoid; B3SAY3; -.
DR OMA; GFKIKPR; -.
DR OrthoDB; 5473721at2759; -.
DR PhylomeDB; B3SAY3; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
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; IBA:GO_Central.
DR GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR CDD; cd18112; ATP-synt_V_A-type_beta_C; 1.
DR CDD; cd18118; ATP-synt_V_A-type_beta_N; 1.
DR CDD; cd01135; V_A-ATPase_B; 1.
DR Gene3D; 3.40.50.12240; -; 1.
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 NCBIfam; TIGR01040; V-ATPase_V1_B; 1.
DR PANTHER; PTHR43389; V-TYPE PROTON ATPASE SUBUNIT B; 1.
DR PANTHER; PTHR43389:SF4; V-TYPE PROTON ATPASE SUBUNIT B; 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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|RuleBase:RU366021};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU366021};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366021}.
FT DOMAIN 29..95
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 152..378
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 496 AA; 55129 MW; 06EBA9833159D85B CRC64;
MDKVSAAKEH VAAVTRNYIT QPRLTYKTVS GVNGPLVILD HVKFPKFAEI VNLTLPDGTK
RSGQVLEVNG SKAVVQVFEG TSGIDAKKTT CEFTGDILRT PVSEDMLGRV FNGSGKAIDK
GPPVLAEDFL DISGQPINPW SRIYPEEMIQ TGISAIDTMN SIARGQKIPI FSAAGLPHND
IAAQICRQAG LVKVNKGIHD DHSDNFAIVF AAMGVNMETA RFFKQDFEEN GSMDNVCLFL
NLANDPTIER IVTPRFALTT AEFFAYQCEK HVLVILTDMS SYAEALREVS AAREEVPGRR
GFPGYMYTDL ATIYERAGRV EGRNGSITQI PILTMPNDDI THPIPDLTGY ITEGQIYVDR
QLHNRQVYPP INVLPSLSRL MKSAIGEGMT RPDHSEVSNQ LYANYAIGKD VQAMKAVVGE
EALTPEDLLY LEFLGKFEKN FISQGSYCVY ENRTVFESLD IGWQLMRIFP REMLKRITKG
TLDEYYSRDS RGAQAK
//
