ID B1L6G8_KORCO Unreviewed; 465 AA.
AC B1L6G8;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
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|HAMAP-Rule:MF_00310};
GN Name=atpB {ECO:0000256|HAMAP-Rule:MF_00310};
GN OrderedLocusNames=Kcr_1301 {ECO:0000313|EMBL:ACB08047.1};
OS Korarchaeum cryptofilum (strain OPF8).
OC Archaea; Candidatus Korarchaeota; Korarchaeum.
OX NCBI_TaxID=374847 {ECO:0000313|EMBL:ACB08047.1, ECO:0000313|Proteomes:UP000001686};
RN [1] {ECO:0000313|EMBL:ACB08047.1, ECO:0000313|Proteomes:UP000001686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OPF8 {ECO:0000313|Proteomes:UP000001686};
RX PubMed=18535141; DOI=10.1073/pnas.0801980105;
RA Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L.,
RA Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A.,
RA Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., Wanner G.,
RA Richardson P., Keller M., Stetter K.O.;
RT "A korarchaeal genome reveals new insights into the evolution of the
RT Archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(2008).
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; CP000968; ACB08047.1; -; Genomic_DNA.
DR RefSeq; WP_012309944.1; NC_010482.1.
DR AlphaFoldDB; B1L6G8; -.
DR STRING; 374847.Kcr_1301; -.
DR EnsemblBacteria; ACB08047; ACB08047; Kcr_1301.
DR GeneID; 6094578; -.
DR KEGG; kcr:Kcr_1301; -.
DR eggNOG; arCOG00865; Archaea.
DR HOGENOM; CLU_022916_0_0_2; -.
DR InParanoid; B1L6G8; -.
DR OrthoDB; 32941at2157; -.
DR PhylomeDB; B1L6G8; -.
DR Proteomes; UP000001686; 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:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
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; 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 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; 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:UP000001686};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00310}.
FT DOMAIN 13..76
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 133..351
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 465 AA; 51950 MW; EA72D4D7CE21F374 CRC64;
MPIRGIAFRG IDQVKGPLVI MRGVPGVAYE EVVRIYSEDG REWLGQVLEA GRDKVVIQIL
GDTEGLDANA IVKFTGSTLK VAVSDEVLGR VFNGAGEPID GGPKIRAEDF RDINGAPINP
VKRDYPDEFI ETGISAIDGM LSLIRGQKLP IFSESGLPHN EVAAQIARQA VVLGREEKFS
IVFAAVGLKY DDVLFFRRQF EEFGALSRSV LFLNLANDPV IERITTPRVA LTVAEYLAFD
LGMDVLVIID DMTNYCEALR ELSSAREEVP SRKGYPGYMY SDLASIYERA GRIIGRPGSI
TFMPILTMPG GDLTHPIPDL TGYITEGQIF LDLDLHNRGI YPPINVLPSL SRLMKDGIGP
GKTREDHKEV SDQLYAAYSQ GTKARELVQI VGEAGLSQRE RLYLEFARRF EREFVSQGFK
ERRTIEETLN IAWDILSVLP ESELTRISEK TISKYHPRRR LLVER
//
