ID A0A0E3KWL1_9EURY Unreviewed; 460 AA.
AC A0A0E3KWL1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
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 ORFNames=MSWH1_0597 {ECO:0000313|EMBL:AKB20868.1};
OS Methanosarcina sp. WH1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=1434102 {ECO:0000313|EMBL:AKB20868.1, ECO:0000313|Proteomes:UP000033112};
RN [1] {ECO:0000313|EMBL:AKB20868.1, ECO:0000313|Proteomes:UP000033112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH1 {ECO:0000313|EMBL:AKB20868.1,
RC ECO:0000313|Proteomes:UP000033112};
RA Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT "Methanogenic archaea and the global carbon cycle.";
RL Submitted (JUL-2014) 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; CP009504; AKB20868.1; -; Genomic_DNA.
DR RefSeq; WP_048126021.1; NZ_CP009504.1.
DR AlphaFoldDB; A0A0E3KWL1; -.
DR GeneID; 24834369; -.
DR KEGG; mef:MSWH1_0597; -.
DR PATRIC; fig|1434102.4.peg.737; -.
DR HOGENOM; CLU_022916_0_0_2; -.
DR Proteomes; UP000033112; 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:AKB20868.1};
KW Ion transport {ECO:0000256|HAMAP-Rule:MF_00310};
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 460 AA; 50206 MW; 7CA6F5DFE892BF49 CRC64;
MVKEYKTITQ IAGPLVFVEK TEPVGYKEIV TVNLPDGTTR RGEVLDSSAD IVVIQIFEGT
TGLDKNCGVV FTGETLKLPA SIDLLGRILS GSGEPLDGGP RIVPDQLLDI NGAAMNPYAR
LPPKDFIQTG ISTIDGTNTL VRGQKLPIFS ASGLPHNEIA LQIARQSAVP GSEAAFAVVF
AAMGITNEEA QYFMSDFEKT GALERAVVFL NLADDPAVER IVTPRMALTA AEYLAYEHGM
HVLVILTDIT NYAEALRQMG AARNEIPGRR GYPGYMYTDL ATLYERAGIV KGAKGSVTQI
PILSMPGDDI THPIPDLSGY ITEGQIVVSR ELHRKGIYPP INVLPSLSRL MNSGIGADKT
REDHKAVSDQ MYAGYAEGRD LRGLVAIVGK EALSDRDVKF LEFADLFEQN FVTQGRNENR
TIADTLDIGW KILAHLPENQ LGRIDNKYIQ KYHPAHRKGQ
//
