ID B8KUD0_9GAMM Unreviewed; 461 AA.
AC B8KUD0;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 64.
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:EED36220.1};
GN ORFNames=NOR51B_2169 {ECO:0000313|EMBL:EED36220.1};
OS Luminiphilus syltensis NOR5-1B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Luminiphilus.
OX NCBI_TaxID=565045 {ECO:0000313|EMBL:EED36220.1, ECO:0000313|Proteomes:UP000004699};
RN [1] {ECO:0000313|Proteomes:UP000004699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NOR51-B {ECO:0000313|Proteomes:UP000004699};
RX PubMed=23705883;
RA Spring S., Riedel T., Sproer C., Yan S., Harder J., Fuchs B.M.;
RT "Taxonomy and evolution of bacteriochlorophyll a-containing members of the
RT OM60/NOR5 clade of marine gammaproteobacteria: description of Luminiphilus
RT syltensis gen. nov., sp. nov., reclassification of Haliea rubra as
RT Pseudohaliea rubra gen. nov., comb. nov., and emendation of Chromatocurvus
RT halotolerans.";
RL BMC Microbiol. 13:118-118(2013).
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. T3SS ATPase
CC subfamily. {ECO:0000256|ARBA:ARBA00024342}.
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DR EMBL; DS999411; EED36220.1; -; Genomic_DNA.
DR AlphaFoldDB; B8KUD0; -.
DR STRING; 565045.NOR51B_2169; -.
DR eggNOG; COG0055; Bacteria.
DR HOGENOM; CLU_022398_0_2_6; -.
DR Proteomes; UP000004699; 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};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01347};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|HAMAP-Rule:MF_01347};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP-
KW Rule:MF_01347}; Hydrolase {ECO:0000313|EMBL:EED36220.1};
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:UP000004699};
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 135..327
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 143..150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01347"
SQ SEQUENCE 461 AA; 49963 MW; 49E425C40C9D5C2C CRC64;
MVQIIGAVID VEFPRESVPQ VYDALTISGK DLTLEVQQQL GDGIVRTIAM GSSEGISRGL
EVENTGAPVS VPVGVETLGR IMDVLGRPID ERGDIGEKER ASIHRDAPAY DELAASEELL
ETGIKVIDLV CPFAKGGKVG LFGGAGVGKT VNMMELINNI ATEHSGLSVF AGVGERTREG
NDFYYEMQES GVVDIENPSN SKVAMVYGQM NEPPGNRLRV ALTGLTMAEK FRDEGRDVLL
FVDNIYRYTL AGTEVSALLG RMPSAVGYQP TLAEEMGVLQ ERITSTKTGS ITSIQAVYVP
ADDLTDPSPA TTFAHLDSTV VLSRDIAAKG IYPAVDPLDS TSRQLDPLVI GNEHYEVARG
VQSVLQRYKE LKDIIAILGM DELSEEDKMT VARARKIERF LSQPFHVAEV FTGSPGIYVS
LKDTIAGFKG LLNGDYDHLP EQAFYMVGSI DQAVERAEKL K
//
