UniProt: A0A1S1NNN4

Database: UniProt
Entry: A0A1S1NNN4_9GAMM

LinkDB:  A0A1S1NNN4_9GAMM 
Original site:  A0A1S1NNN4_9GAMM

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (12)   
   InterPro (8)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
All databases (23)   

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ID   A0A1S1NNN4_9GAMM        Unreviewed;       457 AA.
AC   A0A1S1NNN4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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:QEL12603.1};
GN   ORFNames=BH688_12805 {ECO:0000313|EMBL:OHV08882.1}, FY550_16600
GN   {ECO:0000313|EMBL:QEL12603.1};
OS   Kushneria phosphatilytica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Kushneria.
OX   NCBI_TaxID=657387 {ECO:0000313|EMBL:OHV08882.1, ECO:0000313|Proteomes:UP000179907};
RN   [1] {ECO:0000313|EMBL:OHV08882.1, ECO:0000313|Proteomes:UP000179907}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCWA18 {ECO:0000313|EMBL:OHV08882.1,
RC   ECO:0000313|Proteomes:UP000179907};
RA   Wang C., Qu L.;
RT   "The draft genome suquence of Kushneria sp. YCWA18.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QEL12603.1, ECO:0000313|Proteomes:UP000322553}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCWA18 {ECO:0000313|EMBL:QEL12603.1,
RC   ECO:0000313|Proteomes:UP000322553};
RA   Du G.-X., Qu L.-Y.;
RT   "Complete genome sequence of Kushneria sp. YCWA18, a halophilic phosphate-
RT   solubilizing bacterium isolated from Daqiao saltern in China.";
RL   Submitted (AUG-2019) 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. T3SS ATPase
CC       subfamily. {ECO:0000256|ARBA:ARBA00024342}.
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DR   EMBL; MKZT01000019; OHV08882.1; -; Genomic_DNA.
DR   EMBL; CP043420; QEL12603.1; -; Genomic_DNA.
DR   RefSeq; WP_070980189.1; NZ_MKZT01000019.1.
DR   AlphaFoldDB; A0A1S1NNN4; -.
DR   STRING; 657387.BH688_12805; -.
DR   KEGG; kuy:FY550_16600; -.
DR   OrthoDB; 9801639at2; -.
DR   Proteomes; UP000179907; Unassembled WGS sequence.
DR   Proteomes; UP000322553; 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};
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};
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:UP000179907};
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          139..348
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   BINDING         147..154
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   457 AA;  50050 MW;  065DA88C018975F4 CRC64;
     MSGRIVQIIG AVIDVEFARD EVPRIFDAIR VTDTDTILEV QQQLGDGIVR TIAMGTTEGL
     RRGLEVENTG APISVPVGKK TLGRIMDVLG EPIDERGEIG EEKRSPIHRE APSYADQAAS
     SDLLETGIKV IDLICPFAKG GKVGLFGGAG VGKTVNMMEL IRNIATEHSG YSVFTGVGER
     TREGNDFYYE MQESNVLDKV SLVYGQMNEP PGNRLRVALT GLTIAEEFRD EGRDVLLFID
     NIYRYTLAGT EVSALLGRMP SAVGYQPTLA EEMGMLQERI TSTRTGSITS VQAVYVPADD
     LTDPSPATTF AHLDATVVLA RSIAELGIYP AIDPLDSTSR QLDPLVVGDE HYKVARGVQN
     VLQRYKELKD IIAILGMDEL SDEDKQTVAR ARKIQRFLSQ PFFVAEVFTG APGKYVSLKE
     TIRAFQGILN GEYDELPEQA FYMVGTIDEA IEKAESM
//

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