ID D2REZ9_ARCPA Unreviewed; 468 AA.
AC D2REZ9;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=V-type ATP synthase beta chain {ECO:0000256|ARBA:ARBA00020960, ECO:0000256|HAMAP-Rule:MF_00310};
DE AltName: Full=V-ATPase subunit B {ECO:0000256|ARBA:ARBA00031703, ECO:0000256|HAMAP-Rule:MF_00310};
GN Name=atpB {ECO:0000256|HAMAP-Rule:MF_00310};
GN OrderedLocusNames=Arcpr_1647 {ECO:0000313|EMBL:ADB58693.1};
OS Archaeoglobus profundus (strain DSM 5631 / JCM 9629 / NBRC 100127 / Av18).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=572546 {ECO:0000313|EMBL:ADB58693.1, ECO:0000313|Proteomes:UP000001901};
RN [1] {ECO:0000313|EMBL:ADB58693.1, ECO:0000313|Proteomes:UP000001901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5631 / JCM 9629 / NBRC 100127 / Av18
RC {ECO:0000313|Proteomes:UP000001901};
RX PubMed=21304717;
RA von Jan M., Lapidus A., Del Rio T.G., Copeland A., Tice H., Cheng J.F.,
RA Lucas S., Chen F., Nolan M., Goodwin L., Han C., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Chertkov O., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Saunders E.,
RA Brettin T., Detter J.C., Chain P., Eichinger K., Huber H., Spring S.,
RA Rohde M., Goker M., Wirth R., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Archaeoglobus profundus type strain (AV18).";
RL Stand. Genomic Sci. 2:327-346(2010).
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:0000256|ARBA:ARBA00003103, ECO:0000256|HAMAP-Rule:MF_00310}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_00310}.
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DR EMBL; CP001857; ADB58693.1; -; Genomic_DNA.
DR RefSeq; WP_012941028.1; NC_013741.1.
DR AlphaFoldDB; D2REZ9; -.
DR STRING; 572546.Arcpr_1647; -.
DR PaxDb; 572546-Arcpr_1647; -.
DR GeneID; 8740340; -.
DR KEGG; apo:Arcpr_1647; -.
DR eggNOG; arCOG00865; Archaea.
DR HOGENOM; CLU_022916_0_0_2; -.
DR OrthoDB; 32941at2157; -.
DR Proteomes; UP000001901; Chromosome.
DR GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR005724; ATPase_A1-cplx_bsu.
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 NCBIfam; TIGR01041; ATP_syn_B_arch; 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; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|HAMAP-Rule:MF_00310};
KW Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_00310};
KW Hydrolase {ECO:0000313|EMBL:ADB58693.1};
KW Ion transport {ECO:0000256|HAMAP-Rule:MF_00310};
KW Reference proteome {ECO:0000313|Proteomes:UP000001901};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00310}.
FT DOMAIN 8..73
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 130..348
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 468 AA; 52586 MW; 675AA6483FB6E99C CRC64;
MGKEYKTITD IAGPLVFLEK TEPVAYGELV TITLPDGSTR RGQVLDTAKD FVVVQVFEGT
RGLDKSCSVR FTGDVVKLNC SKDMLGRILS GSGEPIDGGP KIVPEERRPI IGAAINPYAR
QYPREFIQTG ISAIDGMNTL VRGQKLPIFS GSGLPHNDIA LQIARQAKVR GQEEEFAIVF
AAMGITYEEA HQFMKEFERT GALERAVVFL NLASDPAIER LITPRMALTA AEFLAYEYDY
HILVILTDMT NYCEALREIS AAREEVPGRR GYPGYMYTDL ATIYERAGRI RGRKGTITQM
PILTMPGDDI THPIPDLTGY ITEGQIVLSR ELHAKGIYPP IDVLPSLSRL MKEGIGPGMT
REDHKEWNDQ MYAAYAEGVD LRGLVAIVGE EALSERDRRY LKFADEFERR FVNQGKYEDR
DIEYTLDLGW ELLAILPEEE LTKIRPEYIK KYHPKYRKKA ATEEGEAA
//
