ID A0A3A3FXD4_9BURK Unreviewed; 460 AA.
AC A0A3A3FXD4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=D3878_01325 {ECO:0000313|EMBL:RJG00384.1};
OS Noviherbaspirillum sedimenti.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Noviherbaspirillum.
OX NCBI_TaxID=2320865 {ECO:0000313|EMBL:RJG00384.1, ECO:0000313|Proteomes:UP000266327};
RN [1] {ECO:0000313|Proteomes:UP000266327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K1S02-23 {ECO:0000313|Proteomes:UP000266327};
RA Zhu H.;
RL Submitted (SEP-2018) 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:RJG00384.1}.
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DR EMBL; QYUQ01000002; RJG00384.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A3FXD4; -.
DR OrthoDB; 9148544at2; -.
DR Proteomes; UP000266327; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
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 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; 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.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW Rule:MF_00310}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196};
KW Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_00310};
KW Ion transport {ECO:0000256|HAMAP-Rule:MF_00310};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000266327};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00310}.
FT DOMAIN 12..75
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 134..353
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
SQ SEQUENCE 460 AA; 49609 MW; E6A69BD9588433EB CRC64;
MFPRILVEGA ATRIEGPLLF LKRTLDVGLH DAVEVTGRDG RPRIGRVAAI DQDLLTIEVL
ESTSGLGLAD SVVRFLGEPL SFGLGPGILG RVLNGVGQVI DGGPPIAVRG KYAIDGLPLN
PVWRRPPRDF IETGFTTVDL LNSLVRGQKL PIFSGGGLPH ERIAVEIASN ARLRQGGASD
FAIVFAGIGV PYDSAEFFRR SLEQSGALER TALFLNLASD SSTQRLLTPR FALSAAEYLA
FVEGKHVVVI LTDMTNYCEA LREVSSSKGE IPSRKGFPGY MYSDLATLFE RAGCLQGAQG
TLTQLSILTM PSDDITHPIP DLTGYITEGQ IVLSRDLDRR GIYPPVNVLP SLSRLMKDGI
GAGFTHPDHP ALASQLYAAY ARAIQARLLA SVVGEEDLAP TDRQYLAFGT AFEEQAIGQL
RARTLEESME IGWRLLAALP RLELTRLSNA QISAHLAGLA
//