ID A0A0Q0VZJ0_9EURY Unreviewed; 465 AA.
AC A0A0Q0VZJ0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=APR55_02805 {ECO:0000313|EMBL:KQC09423.1};
OS Methanolinea sp. SDB.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanolinea.
OX NCBI_TaxID=1735327 {ECO:0000313|EMBL:KQC09423.1, ECO:0000313|Proteomes:UP000050878};
RN [1] {ECO:0000313|EMBL:KQC09423.1, ECO:0000313|Proteomes:UP000050878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDB {ECO:0000313|EMBL:KQC09423.1};
RA Wawrik B., Marks C.R., Davidova I.A., Mcinerney M.J., Pruitt S., Duncan K.,
RA Suflita J.M., Callaghan A.V.;
RT "Metagenomic Analysis of a Methanogenic Paraffin-Utilizing Consortium.";
RL Submitted (OCT-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQC09423.1}.
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DR EMBL; LKUF01000154; KQC09423.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q0VZJ0; -.
DR Proteomes; UP000050878; Unassembled WGS sequence.
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; 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 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.
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:KQC09423.1};
KW Ion transport {ECO:0000256|HAMAP-Rule:MF_00310};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00310}.
FT DOMAIN 17..80
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 137..355
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 465 AA; 51697 MW; 3F9BFB9FCC95A6F0 CRC64;
MRSDPLMSRD YRTINYVSGP IMFVQNPIGV SYGETARITL PDGEIRTGQV LDISREMAVV
QVFEGTSGVD NSVTNIRFTG EAAQIDVSID MLGRIFNGVG LPRDGRPNII PEDTVDIAGT
AINPYARDKP SDFIQTGVSA IDALNTLVRG QKLPIFSGSG LPANQLAAQI ARQSRVLGEG
EQFAVVFVAM GITYKEASFF MNDFERTGAL ERVVFFMNLA DDPTIERIAT PRCALSVAEY
LAFTHNLHVL VILTDMTNYC EALREISTAR EEVPGRRGYP GYMYTDLASI YERAGRIKGK
TGSITQIPIL TMPDDDITHP VPDLTGYITE GQIVLSRDLF RRGAEPPIDS LPCLSRLMNL
GIGPGKTRED HRNVADQLYA SYAYGRDLRR LVAIVGEEAL TELDKKYLSF ADQFERRFIS
QGDENRSIEQ TLALGWDLMA SLPEDELKRI KVEYIKRYHP AYRAG
//
