VATB_ANADF
ID VATB_ANADF Reviewed; 460 AA.
AC A7HDG8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=V-type ATP synthase beta chain {ECO:0000255|HAMAP-Rule:MF_00310};
DE AltName: Full=V-ATPase subunit B {ECO:0000255|HAMAP-Rule:MF_00310};
GN Name=atpB {ECO:0000255|HAMAP-Rule:MF_00310};
GN OrderedLocusNames=Anae109_2563;
OS Anaeromyxobacter sp. (strain Fw109-5).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter;
OC unclassified Anaeromyxobacter.
OX NCBI_TaxID=404589;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fw109-5;
RX PubMed=25614562; DOI=10.1128/genomea.01449-14;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA Loeffler F.E., Fields M.W.;
RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT metal-reducing bacterium isolated from a contaminated subsurface
RT environment.";
RL Genome Announc. 3:0-0(2015).
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:0000255|HAMAP-Rule:MF_00310}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_00310}.
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DR EMBL; CP000769; ABS26764.1; -; Genomic_DNA.
DR RefSeq; WP_012097358.1; NC_009675.1.
DR AlphaFoldDB; A7HDG8; -.
DR SMR; A7HDG8; -.
DR STRING; 404589.Anae109_2563; -.
DR EnsemblBacteria; ABS26764; ABS26764; Anae109_2563.
DR KEGG; afw:Anae109_2563; -.
DR eggNOG; COG1156; Bacteria.
DR HOGENOM; CLU_022916_0_0_7; -.
DR OMA; GFKIKPR; -.
DR OrthoDB; 875807at2; -.
DR Proteomes; UP000006382; 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:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
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; 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; PTHR43389; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Hydrogen ion transport; Ion transport; Reference proteome;
KW Transport.
FT CHAIN 1..460
FT /note="V-type ATP synthase beta chain"
FT /id="PRO_1000059364"
SQ SEQUENCE 460 AA; 50069 MW; A101C6C7BB662001 CRC64;
MDLVTRRVRG ADAIAGPLLF LEGVPRARLG ELVRIRMAGG EERRGQIIEL SGARVAVQVL
EETRGLAPAR AEVTLTGEVA TLAVSRGMLG RVLDGLGRPT DGLPAPIAEA RLPIHGAALN
VTRREKPADF IETGVSAIDG LNTLVRGQKL PVFSCAGLPA GRLAGQIVCQ ARVRGGERFA
VVFAAMGAPF REYDAYLEAF RRAGVLDRTA VFLNRAEDPP IERLMTPRCA LTCAEHLAFS
HGLHVLVVLT DMTSYCEALR EVALARDEVP GRRGYPGYMY TDLATIYERA GRIAGRPGSI
TQVPVLTMPD DDLTHPIPDL SGYITEGQIV LSRELDRRGV YPPIDVLPSL SRLMGLGAGP
GRTRADHRPL ADQLYALYAR GRDVRRMAAI VGSANLGEEE RRLLEFGDRF ERELVGQGDA
FRSIEDTLET GWRLLAQLPP EALARIPAAV LEARRKEGQR