ID A0A1D3L492_9EURY Unreviewed; 463 AA.
AC A0A1D3L492;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 ECO:0000313|EMBL:SCG86451.1};
GN ORFNames=MCBB_1902 {ECO:0000313|EMBL:SCG86451.1};
OS Methanobacterium congolense.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX NCBI_TaxID=118062 {ECO:0000313|EMBL:SCG86451.1, ECO:0000313|Proteomes:UP000094707};
RN [1] {ECO:0000313|EMBL:SCG86451.1, ECO:0000313|Proteomes:UP000094707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Buetzberg {ECO:0000313|EMBL:SCG86451.1};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) 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: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; LT607756; SCG86451.1; -; Genomic_DNA.
DR RefSeq; WP_071907514.1; NZ_LT607756.1.
DR AlphaFoldDB; A0A1D3L492; -.
DR STRING; 118062.MCBB_1902; -.
DR GeneID; 30412741; -.
DR KEGG; mcub:MCBB_1902; -.
DR PATRIC; fig|129848.4.peg.1949; -.
DR OrthoDB; 32941at2157; -.
DR Proteomes; UP000094707; Chromosome I.
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: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; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
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; SSF50615; N-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 Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_00310}; Reference proteome {ECO:0000313|Proteomes:UP000094707};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00310}.
FT DOMAIN 13..79
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 136..354
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 463 AA; 51569 MW; 3E3DFF35E56E694C CRC64;
MKIDIKTREY TTVSEVSGPL MIVEGVEGVA YNEIVEIETP AGENRRGQVL EVKDDLAVVQ
VFEGTSDLNT ATTKVRFTGE TAKLGVSPDM LGRIFNGTGK PIDGGPEIIP EEELDINGNP
MNPSAREFPA EFIETGISTI DGMNTLVRGQ KLPIFSGSGL PHNELAAQIA RQAKVIGEGS
EFAVIFAAMG ITHEEANYFM RDFERTGALE RVTVFMNLAD DPAIERIITP KMALTTAEYF
AFEKNMHVLV ILTDLTNYCE ALREISAARD EVPGRRGYPG YMYTDLATMY ERAGRILGKE
GSITQMPILV MPQDDITHPI PDLTGYITEG QIVLSRDLHR KGIYPPVDVL PSLSRLMSGG
IGEGQTREDH SGVSDQLYSA YAEGRELRDL MAVVGEEALT ERDRKFLKFA DEFEKQFITQ
TRDEDRSIEE TLTLGWELLA LLPKAELKRV REEHIPKYHP EYK
//
