GenomeNet

Database: UniProt
Entry: A0A3A3FXD4_9BURK
LinkDB: A0A3A3FXD4_9BURK
Original site: A0A3A3FXD4_9BURK 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system