UniProt: A0A2C6DB34

Database: UniProt
Entry: A0A2C6DB34_9GAMM

LinkDB:  A0A2C6DB34_9GAMM 
Original site:  A0A2C6DB34_9GAMM

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (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 (22)   

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ID   A0A2C6DB34_9GAMM        Unreviewed;       459 AA.
AC   A0A2C6DB34;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-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:PHI28426.1};
GN   ORFNames=CRN84_03330 {ECO:0000313|EMBL:PHI28426.1}, NCTC12282_01250
GN   {ECO:0000313|EMBL:VFS46341.1};
OS   Budvicia aquatica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Budviciaceae; Budvicia.
OX   NCBI_TaxID=82979 {ECO:0000313|EMBL:PHI28426.1, ECO:0000313|Proteomes:UP000224974};
RN   [1] {ECO:0000313|Proteomes:UP000224974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FDAARGOS_387 {ECO:0000313|Proteomes:UP000224974};
RA   Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA   Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA   Nadendla S., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PHI28426.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FDAARGOS_387 {ECO:0000313|EMBL:PHI28426.1};
RA   Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.J.,
RA   Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA   Nadendla S., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:VFS46341.1, ECO:0000313|Proteomes:UP000373449}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC12282 {ECO:0000313|EMBL:VFS46341.1,
RC   ECO:0000313|Proteomes:UP000373449};
RG   Pathogen Informatics;
RL   Submitted (MAR-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; PDDX01000001; PHI28426.1; -; Genomic_DNA.
DR   EMBL; CAADJA010000002; VFS46341.1; -; Genomic_DNA.
DR   RefSeq; WP_029094795.1; NZ_PDDX01000001.1.
DR   AlphaFoldDB; A0A2C6DB34; -.
DR   STRING; 1111728.GCA_000427805_02065; -.
DR   OrthoDB; 9801639at2; -.
DR   Proteomes; UP000224974; Unassembled WGS sequence.
DR   Proteomes; UP000373449; 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:VFS46341.1};
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:UP000224974};
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          141..326
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   BINDING         149..156
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01347"
SQ   SEQUENCE   459 AA;  49965 MW;  771945E3DB056FD7 CRC64;
     MATGKIIQVI GAVVDVEFPQ DAVPKVYDAL EVQNDVKLVL EVQQQLGGGV VRCIAMGTSD
     GLSRGLKVLD LEHPIEVPVG VATLGRIMNV LGEPIDMKGD IGEEERWAIH RAAPSYEDLS
     SANELLETGI KVIDLICPFA KGGKVGLFGG AGVGKTVNMM ELIRNIATEH SGYSVFAGVG
     ERTREGNDFY HEMTESNVLD KVSLVYGQMN EPPGNRLRVA LTGLTMAEKF RDEGRDVLLF
     IDNIYRYTLA GTEVSALLGR MPSAVGYQPT LAEEMGTLQE RITSTKTGSI TSVQAVYVPA
     DDLTDPSPAT TFAHLDATVV LSRQIASLGI YPAVDPLDST SRQLDPLVVG QEHYDCARGV
     QSILQRYQEL KDIIAILGMD ELSESDKLVV SRARKIQRFL SQPFFVAEVF TGSSGKYVSL
     KDTIRGFNGI MNGEYDHLPE QAFYMVGSIE EAVEKAKKL
//

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