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Database: UniProt
Entry: R7RQW3_9CLOT
LinkDB: R7RQW3_9CLOT
Original site: R7RQW3_9CLOT 
ID   R7RQW3_9CLOT            Unreviewed;       455 AA.
AC   R7RQW3;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=TCEL_00623 {ECO:0000313|EMBL:CDF58577.1};
OS   Thermobrachium celere DSM 8682.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Thermobrachium.
OX   NCBI_TaxID=941824 {ECO:0000313|EMBL:CDF58577.1, ECO:0000313|Proteomes:UP000014923};
RN   [1] {ECO:0000313|EMBL:CDF58577.1, ECO:0000313|Proteomes:UP000014923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8682 {ECO:0000313|EMBL:CDF58577.1,
RC   ECO:0000313|Proteomes:UP000014923};
RA   Ciranna A., Larjo A., Kivisto A., Santala V., Roos C., Karp M.;
RT   "Draft genome sequence of the hydrogen-ethanol-producing anaerobic
RT   alkalithermophilic Caloramator celere.";
RL   Submitted (MAR-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:CDF58577.1}.
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DR   EMBL; CAVN010000097; CDF58577.1; -; Genomic_DNA.
DR   RefSeq; WP_018662829.1; NZ_HF952018.1.
DR   AlphaFoldDB; R7RQW3; -.
DR   eggNOG; COG1156; Bacteria.
DR   HOGENOM; CLU_022916_0_0_9; -.
DR   OrthoDB; 9802718at2; -.
DR   Proteomes; UP000014923; Unassembled WGS sequence.
DR   GO; GO:0045259; C:proton-transporting ATP synthase complex; IEA:UniProt.
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; 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:SF4; ATP-SYNT_AB DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR43389; 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   Hydrolase {ECO:0000313|EMBL:CDF58577.1};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_00310}; Reference proteome {ECO:0000313|Proteomes:UP000014923};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00310}.
FT   DOMAIN          11..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   455 AA;  50925 MW;  026BEBDE0C91A2E9 CRC64;
     MYKEYLSLKK IEGPLIVVEG VKGVSYNEMV EIKLKDKIKH GKVVQLNGDI AVIQVFENTS
     GMSVRDISVK FTGKPLEIKL SREILGRIFN GIGEPIDGGG PIFNGIKLDV NGSPINPVAR
     RYPRNYIQTG ISAIDTLTTL IRGQKLPIFS GNGLPHNQIA AQIVKQARVA EGEGEFAVVF
     AAMGIKHDDA HYFIKAFQDA GVLDRVVMFM NLADDPVVER IVTPRCALTA AEYLAFYENM
     HILVIMTDIT SYCEALREIS AAREEVPGRK GYPGYLYSDL ASLYERAGMV EGSKGSITQI
     PILTMPNDDI THPIPDLTGY ITEGQIVLSR EIYQRNIYPP INILPSLSRL MKDGIGEGYT
     RADHPDVANQ IFSSYSKVQE VKALSQVIGE DELSEIDKKY LEFGNAFEYR FLKQSFDEDR
     DVKESLDIAW EILSILPKNE LDRINPKFID EYYRG
//
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