ID A0A011WPR7_RUMAL Unreviewed; 462 AA.
AC A0A011WPR7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=V-type ATP synthase beta chain {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 ORFNames=RASY3_11820 {ECO:0000313|EMBL:EXM38985.1};
OS Ruminococcus albus SY3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=1341156 {ECO:0000313|EMBL:EXM38985.1, ECO:0000313|Proteomes:UP000021369};
RN [1] {ECO:0000313|EMBL:EXM38985.1, ECO:0000313|Proteomes:UP000021369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY3 {ECO:0000313|EMBL:EXM38985.1,
RC ECO:0000313|Proteomes:UP000021369};
RA Dassa B., Borovok I., Lamed R., Flint H., Yeoman C.J., White B.,
RA Bayer E.A.;
RT "Rumen cellulosomics: divergent fiber-degrading strategies revealed by
RT comparative genome-wide analysis of six Ruminococcal strains.";
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The V-type beta chain is a regulatory subunit.
CC {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:EXM38985.1}.
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DR EMBL; JEOB01000003; EXM38985.1; -; Genomic_DNA.
DR RefSeq; WP_037288392.1; NZ_JEOB01000003.1.
DR AlphaFoldDB; A0A011WPR7; -.
DR PATRIC; fig|1341156.4.peg.2302; -.
DR OrthoDB; 9802718at2; -.
DR Proteomes; UP000021369; 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 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:EXM38985.1};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_00310}; Reference proteome {ECO:0000313|Proteomes:UP000021369};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00310}.
FT DOMAIN 9..65
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 131..350
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 462 AA; 51134 MW; 5963019A26476719 CRC64;
MNIKYIGLSE INGPLVVLDK CKNVSYDEIA DIELDNGTHR LARVVEVYED KAVLQVFEGT
KGLSLKNTTT SFEGRPMELP LGGEMLGRIF NGAGKPIDGL GEIVAEEYRD INGEPLNPVS
RVYPRNYINT GISSIDALMT LIRGQKLPIF SGSGLSHNKL AVQIVRQAKI ADEAGQDFAV
VFGAMGVTND VADYFRRSFE ETGVLQRVSM FLNLSNDPII ERILTPRCAL TCAEYLAFKK
NMHILVILTD MTSYAEALRE FSSSKGEIPG RKGYPGYLYS DLASIYERAG IVKGANGSVT
QIPILTMPND DITHPVPDLT GYITEGQIVL DRNLDATGVY PGVAILPSLS RLMKDGIGEG
YTREDHQMCA NQLFAAYAKV QDARSLASVI GEEELTATDK AYLRFGELFE AHFIDQGFET
NRSIEETLDL GWKLLSSLPR TELDRVDDEH LDKFYDPENA YK
//
