ID A0A0M1JAT4_9GAMM Unreviewed; 459 AA.
AC A0A0M1JAT4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=TI05_14050 {ECO:0000313|EMBL:KOR30408.1};
OS Achromatium sp. WMS3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Achromatium.
OX NCBI_TaxID=1604836 {ECO:0000313|EMBL:KOR30408.1, ECO:0000313|Proteomes:UP000036918};
RN [1] {ECO:0000313|EMBL:KOR30408.1, ECO:0000313|Proteomes:UP000036918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WMS3 {ECO:0000313|EMBL:KOR30408.1};
RX PubMed=26322031; DOI=10.3389/fmicb.2015.00822;
RA Mansor M., Hamilton T.L., Fantle M.S., Macalady J.L.;
RT "Metabolic diversity and ecological niches of Achromatium populations
RT revealed with single-cell genomic sequencing.";
RL Front. Microbiol. 6:822-822(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:0000256|HAMAP-Rule:MF_00310}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. T3SS ATPase
CC subfamily. {ECO:0000256|ARBA:ARBA00024342}.
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:KOR30408.1}.
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DR EMBL; JXSO01000420; KOR30408.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M1JAT4; -.
DR PATRIC; fig|1604836.3.peg.2878; -.
DR Proteomes; UP000036918; 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; 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:KOR30408.1};
KW Ion transport {ECO:0000256|HAMAP-Rule:MF_00310};
KW Reference proteome {ECO:0000313|Proteomes:UP000036918};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00310}.
FT DOMAIN 14..65
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 132..350
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 459 AA; 50438 MW; D2245B83E41B6EEA CRC64;
MSAKEYRTAS AARGGLLVVS NVPGVAFGDR VQIRDDAGNN RNGQVIRCSN EEVLIQVYEG
TDDINLESTW IRFLDEPLQI ALSPEILGRI FNGIGEPKDN RPPIVSSVLR PVGAGAINPA
ARTYPKEFIQ TGVSTIDGLN SLVRGQKLPI FSGSGLPHNR LAAQIVRQAK LVDQESSFSV
VFAAMGVSNT DAKFFEDAFA DSGVLGNVVM FVNLADDPPI ERLALPRVAL TAAEYLAFDL
DRHVLVVMTD LTYYAEALRE VATAKGDVPS RKGYPGYLYS DLAEIYERCG RIKGRTGSIT
LVPVVSMPSD DITHPIPDLT GYITEGQIVL NRELHSQGIY PPVHVSSSLS RLMKDGIGKD
DTRDDHPHVA SQLFALYARA LETRNLASII GADELSERDR RYLQFADAFD SRFVGQKETE
DRSIIDTLDL SWELLSMFPK DALSRVSETE IAKYYNPAE
//
