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Protein

ATP synthase subunit beta

Gene

atpD

Organism
Bacillus anthracis
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.UniRule annotation

Catalytic activityi

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi156 – 1638ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciANTHRA:ATPD-MONOMER.
BANT260799:GJAJ-5230-MONOMER.
BANT261594:GJ7F-5408-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit betaUniRule annotation (EC:3.6.3.14UniRule annotation)
Alternative name(s):
ATP synthase F1 sector subunit betaUniRule annotation
F-ATPase subunit betaUniRule annotation
Gene namesi
Name:atpDUniRule annotation
Ordered Locus Names:BA_5547, GBAA_5547, BAS5155
OrganismiBacillus anthracis
Taxonomic identifieri1392 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000000594 Componenti: Chromosome

Subcellular locationi

  • Cell membrane UniRule annotation; Peripheral membrane protein UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, CF(1), Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 469469ATP synthase subunit betaPRO_0000254205Add
BLAST

Proteomic databases

PRIDEiQ81JZ5.

Interactioni

Subunit structurei

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a1, b2 and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF1 is attached to CF0 by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains.UniRule annotation

Protein-protein interaction databases

STRINGi198094.BA_5547.

Structurei

3D structure databases

ProteinModelPortaliQ81JZ5.
SMRiQ81JZ5. Positions 1-467.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C4J. Bacteria.
COG0055. LUCA.
HOGENOMiHOG000009605.
KOiK02112.
OMAiAEFGIYP.
OrthoDBiEOG6HQSP3.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact.
InterProiIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q81JZ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKGRVTQIM GPVVDVKFDG GKLPEIYNAL TVKQSNENGT SINLTFEVAL
60 70 80 90 100
HLGDDTVRTV AMSSTDGLVR GTEVEDTGKA ISVPVGDATL GRVFNVLGDA
110 120 130 140 150
IDLDGEVPAD VRRDPIHRQA PAFEELSTKV EILETGIKVV DLLAPYIKGG
160 170 180 190 200
KIGLFGGAGV GKTVLIQELI NNIAQEHGGI SVFAGVGERT REGNDLYHEM
210 220 230 240 250
SDSGVIKKTA MVFGQMNEPP GARQRVALTG LTMAEHFRDE QGQDVLLFID
260 270 280 290 300
NIFRFTQAGS EVSALLGRMP SAVGYQPTLA TEMGQLQERI TSTNKGSITS
310 320 330 340 350
IQAVYVPADD YTDPAPATTF AHLDATTNLE RRLTQMGIYP AVDPLASTSR
360 370 380 390 400
ALSPEIVGEE HYEVARQVQQ TLQRYKELQD IIAILGMDEL SEEDKLVVHR
410 420 430 440 450
ARRIQFFLSQ NFHVAEQFTG QKGSYVPVKE TVRGFKEILE GKYDDLPEDA
460
FRLVGGIEEV IENAKKMMA
Length:469
Mass (Da):51,194
Last modified:June 1, 2003 - v1
Checksum:iA4EEA00A9B1E6E9F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP29191.1.
AE017225 Genomic DNA. Translation: AAT57444.1.
AE017334 Genomic DNA. Translation: AAT34691.1.
RefSeqiNP_847705.1. NC_003997.3.
WP_001032600.1. NZ_LHUO01000009.1.
YP_031394.1. NC_005945.1.

Genome annotation databases

EnsemblBacteriaiAAP29191; AAP29191; BA_5547.
AAT34691; AAT34691; GBAA_5547.
AAT57444; AAT57444; BAS5155.
GeneIDi1085230.
2852682.
KEGGiban:BA_5547.
bar:GBAA_5547.
bat:BAS5155.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016879 Genomic DNA. Translation: AAP29191.1.
AE017225 Genomic DNA. Translation: AAT57444.1.
AE017334 Genomic DNA. Translation: AAT34691.1.
RefSeqiNP_847705.1. NC_003997.3.
WP_001032600.1. NZ_LHUO01000009.1.
YP_031394.1. NC_005945.1.

3D structure databases

ProteinModelPortaliQ81JZ5.
SMRiQ81JZ5. Positions 1-467.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198094.BA_5547.

Proteomic databases

PRIDEiQ81JZ5.

Protocols and materials databases

DNASUi1085230.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP29191; AAP29191; BA_5547.
AAT34691; AAT34691; GBAA_5547.
AAT57444; AAT57444; BAS5155.
GeneIDi1085230.
2852682.
KEGGiban:BA_5547.
bar:GBAA_5547.
bat:BAS5155.

Phylogenomic databases

eggNOGiENOG4105C4J. Bacteria.
COG0055. LUCA.
HOGENOMiHOG000009605.
KOiK02112.
OMAiAEFGIYP.
OrthoDBiEOG6HQSP3.

Enzyme and pathway databases

BioCyciANTHRA:ATPD-MONOMER.
BANT260799:GJAJ-5230-MONOMER.
BANT261594:GJ7F-5408-MONOMER.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact.
InterProiIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
    Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J.
    , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
    Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames / isolate Porton.
  2. "Complete genome sequence of Bacillus anthracis Sterne."
    Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sterne.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames ancestor.

Entry informationi

Entry nameiATPB_BACAN
AccessioniPrimary (citable) accession number: Q81JZ5
Secondary accession number(s): Q6HQJ4, Q6KJW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: June 1, 2003
Last modified: May 11, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.