ID VATB_PYRCJ Reviewed; 467 AA.
AC A3MU07;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=V-type ATP synthase beta chain {ECO:0000255|HAMAP-Rule:MF_00310};
DE AltName: Full=V-ATPase subunit B {ECO:0000255|HAMAP-Rule:MF_00310};
GN Name=atpB {ECO:0000255|HAMAP-Rule:MF_00310}; OrderedLocusNames=Pcal_0698;
OS Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=410359;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21063 / JCM 11548 / VA1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The archaeal beta chain is a regulatory subunit.
CC {ECO:0000255|HAMAP-Rule:MF_00310}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_00310}.
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DR EMBL; CP000561; ABO08124.1; -; Genomic_DNA.
DR AlphaFoldDB; A3MU07; -.
DR SMR; A3MU07; -.
DR STRING; 410359.Pcal_0698; -.
DR KEGG; pcl:Pcal_0698; -.
DR eggNOG; arCOG00865; Archaea.
DR HOGENOM; CLU_022916_0_0_2; -.
DR OrthoDB; 32941at2157; -.
DR Proteomes; UP000001431; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
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; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022879; V-ATPase_su_B/beta.
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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Hydrogen ion transport; Ion transport; Transport.
FT CHAIN 1..467
FT /note="V-type ATP synthase beta chain"
FT /id="PRO_1000059388"
FT REGION 95..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 51973 MW; ADDDA124CB76923C CRC64;
MLTPVVSYST VREVKGPLLV IERTRGVSYG EIGEVVGPDG EPRKVQVIEV ATDYAVAQVL
GGTLGLPSKG STVRFYGKTL KIPVSEQLIG RILDGKGQPR DHMPLPPPED FRDVNGEPLN
PYSREYPEEP IETGISAIDG LYTLVRGQKL PIFSGTGLPH NMMAAQVVRQ STVRGSGEEF
AVVFVGIGIK TEEALFFMDE FRKTGALRRA VAVINLASDP VAERILAPRV GLTIAEYLAW
QLGYHVLVVM TDMTNYCEGL RELSSGKGEL PGRRGYPGYM YTDLATIYER AGKAHGKKGS
VTQFPILTMP NDDITHPIPD LTGYITEGQL VLSRAMWGKG IYPPFDVIMS LSRLAKDAIG
EGKTREDHKD VANTLIAAYS KALELRNLAT LVGERNLGWR ERRYLRFADA FEQKFIKQGY
YERRSFEETL DIGWDVLSIL PEDELTNARP QITQKFYRRH IFESVAV
//
