ID W8GEL8_9MOLU Unreviewed; 457 AA.
AC W8GEL8;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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 ECO:0000313|EMBL:AHK22244.1};
GN ORFNames=X271_00135 {ECO:0000313|EMBL:AHK22244.1};
OS Candidatus Hepatoplasma crinochetorum Av.
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Hepatoplasma.
OX NCBI_TaxID=1427984 {ECO:0000313|EMBL:AHK22244.1, ECO:0000313|Proteomes:UP000019450};
RN [1] {ECO:0000313|EMBL:AHK22244.1, ECO:0000313|Proteomes:UP000019450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Av {ECO:0000313|EMBL:AHK22244.1,
RC ECO:0000313|Proteomes:UP000019450};
RX PubMed=24482531; DOI=10.1093/gbe/evu020;
RA Leclercq S., Dittmer J., Bouchon D., Cordaux R.;
RT "Phylogenomics of "Candidatus Hepatoplasma crinochetorum," a Lineage of
RT Mollicutes Associated with Noninsect Arthropods.";
RL Genome Biol. Evol. 6:407-415(2014).
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}.
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DR EMBL; CP006932; AHK22244.1; -; Genomic_DNA.
DR AlphaFoldDB; W8GEL8; -.
DR STRING; 1427984.X271_00135; -.
DR KEGG; hcr:X271_00135; -.
DR PATRIC; fig|1427984.3.peg.125; -.
DR eggNOG; COG0055; Bacteria.
DR HOGENOM; CLU_022398_0_2_14; -.
DR OrthoDB; 9801639at2; -.
DR Proteomes; UP000019450; Chromosome.
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 Hydrolase {ECO:0000313|EMBL:AHK22244.1};
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:UP000019450};
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 144..330
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 152..159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01347"
SQ SEQUENCE 457 AA; 50091 MW; D4D343630D0EB0F9 CRC64;
MKNIGKISQI LGPVVDVKFT NTKVPDILNA LEIIVNKNKK IVLEVASILG DDVVRCISMS
PTEGLRRGLD VIDTGSPIRV PVGNETLGRI FNVLGEPVDE KPISKNVLRM PIHRQAPNYS
EQATTTELFE TGIKVIDLLL PFAKGSKVGL LGGAGVGKTV LIQELINNVA QEHGGISVFT
GVGERTREGN DLYFEMKESG VLSKTALAFG QMNEPPGARM RVALTGLTMA EYFRDEKKQD
VLLFIDNIFR FSQAGAEVSA LLGRMPSAVG YQPTLSIDMG KLQERITSTK KGSITSVQAI
FVPADDLTDP APATTFSHLD ASIVLSRQIA SLGLYPALDP LESNSSLLDP DIVGQEHYDV
ASRVLEILQR YKELQDIIAI LGMDELSDED KQIVTRARKI RNFLTQPFHV AEQFSGKKGV
FVKINDTIQG FKEIIEGKHD QKSESIFLYK GKISEVK
//
