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Database: UniProt
Entry: A0A0P7AXK3_9FLAO
LinkDB: A0A0P7AXK3_9FLAO
Original site: A0A0P7AXK3_9FLAO 
ID   A0A0P7AXK3_9FLAO        Unreviewed;       502 AA.
AC   A0A0P7AXK3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=ATP synthase subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
DE            EC=7.1.2.2 {ECO:0000256|HAMAP-Rule:MF_01347};
DE   AltName: Full=ATP synthase F1 sector subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
DE   AltName: Full=F-ATPase subunit beta {ECO:0000256|HAMAP-Rule:MF_01347};
GN   Name=atpD {ECO:0000256|HAMAP-Rule:MF_01347};
GN   ORFNames=I595_1333 {ECO:0000313|EMBL:KPM32906.1};
OS   Croceitalea dokdonensis DOKDO 023.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Croceitalea.
OX   NCBI_TaxID=1300341 {ECO:0000313|EMBL:KPM32906.1, ECO:0000313|Proteomes:UP000050280};
RN   [1] {ECO:0000313|EMBL:KPM32906.1, ECO:0000313|Proteomes:UP000050280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DOKDO 023 {ECO:0000313|EMBL:KPM32906.1,
RC   ECO:0000313|Proteomes:UP000050280};
RA   Kwon S.-K., Lee H.K., Kwak M.-J., Kim J.F.;
RT   "Genome sequence of the marine flavobacterium Croceitalea dokdonensis DOKDO
RT   023 that contains proton- and sodium-pumping rhodopsins.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The catalytic sites are hosted primarily by the
CC       beta subunits. {ECO:0000256|HAMAP-Rule:MF_01347}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01347};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01347};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01347}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_01347}.
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:KPM32906.1}.
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DR   EMBL; LDJX01000002; KPM32906.1; -; Genomic_DNA.
DR   RefSeq; WP_054558705.1; NZ_LDJX01000002.1.
DR   AlphaFoldDB; A0A0P7AXK3; -.
DR   STRING; 1300341.I595_1333; -.
DR   PATRIC; fig|1300341.3.peg.1529; -.
DR   OrthoDB; 9801639at2; -.
DR   Proteomes; UP000050280; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   CDD; cd18110; ATP-synt_F1_beta_C; 1.
DR   CDD; cd18115; ATP-synt_F1_beta_N; 1.
DR   CDD; cd01133; F1-ATPase_beta_CD; 1.
DR   Gene3D; 2.40.10.170; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR005722; ATP_synth_F1_bsu.
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; IPR024034; ATPase_F1/V1_b/a_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR01039; atpD; 1.
DR   PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR   PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   SMART; SM00382; AAA; 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|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW   Rule:MF_01347};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01347}; Cell membrane {ECO:0000256|HAMAP-Rule:MF_01347};
KW   CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|HAMAP-Rule:MF_01347};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01347};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_01347};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01347};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01347}; Reference proteome {ECO:0000313|Proteomes:UP000050280};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW   Rule:MF_01347};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01347}.
FT   DOMAIN          148..365
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   BINDING         156..163
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   502 AA;  54117 MW;  8D8297958825F1E4 CRC64;
     MAKVTGKVAQ IIGPVIDVEF ESGTEIPKIY DSLEIVKADG YKLVLEVQSH VGENTVRTIS
     MDSTDGLSRG AEAVATGSAI QMPIGEEVYG RLFNVIGDAI DGMENLPKAG ENGLPIHREA
     PKFEDLSTST EVLFTGIKVI DLIEPYAKGG KIGLFGGAGV GKTVLIQELI NNIAKGHGGL
     SVFAGVGERT REGNDLLREM LESGIIKYGD DFLHSMEEGG WDLSKVDKTA MKESKATFVF
     GQMNEPPGAR ARVALSGLTI AEYFRDGAGD GQGKDVLFFV DNIFRFTQAG SEVSALLGRM
     PSAVGYQPTL ATEMGAMQER ITSTKRGSIT SVQAVYVPAD DLTDPAPATT FAHLDATTVL
     SRKIAELGIY PAVDPLDSTS RILTPEILGA DHYSCAQRVK ELLQRYKELQ DIIAILGMEE
     LSEEDKLAVG RARRVQRFLS QPFHVAEQFT GIPGVLVDIK ETIKGFNMIM DGELDHLPES
     AFNLKGTIEE AIEAGEKMLA EA
//
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