Skip Header

Contribute Send feedback
Read comments (?) or add your own

P99112 (ATPB_STAAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase subunit beta
EC=3.6.3.14
Alternative name(s):
ATP synthase F1 sector subunit beta
F-ATPase subunit beta
Gene names
Name:atpD
Ordered Locus Names:SA1905
OrganismStaphylococcus aureus (strain N315) [Complete proteome] [HAMAP]
Taxonomic identifier158879 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus ›

Protein attributes

Sequence length470 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits By similarity. HAMAP-Rule MF_01347

Catalytic activity

ATP + H2O + H+(In) = ADP + phosphate + H+(Out). HAMAP-Rule MF_01347

Subunit structure

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 By similarity.

Subcellular location

Cell membrane; Peripheral membrane protein By similarity HAMAP-Rule MF_01347.

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 470470ATP synthase subunit beta HAMAP-Rule MF_01347
PRO_0000144470

Regions

Nucleotide binding155 – 1628ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P99112 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: C388E63D87E7F488

FASTA47051,400
        10         20         30         40         50         60 
MGIGRVTQVM GPVIDVRFEH NEVPKINNAL VIDVPKEEGT IQLTLEVALQ LGDDVVRTIA 

        70         80         90        100        110        120 
MDSTDGVQRG MDVKDTGKEI SVPVGDETLG RVFNVLGETI DLKEEISDSV RRDPIHRQAP 

       130        140        150        160        170        180 
AFDELSTEVQ ILETGIKVVD LLAPYIKGGK IGLFGGAGVG KTVLIQELIN NIAQEHGGIS 

       190        200        210        220        230        240 
VFAGVGERTR EGNDLYFEMS DSGVIKKTAM VFGQMNEPPG ARMRVALSGL TMAEYFRDEQ 

       250        260        270        280        290        300 
GQDVLLFIDN IFRFTQAGSE VSALLGRMPS AVGYQPTLAT EMGQLQERIT STTKGSVTSI 

       310        320        330        340        350        360 
QAVFVPADDY TDPAPATAFA HLDATTNLER KLTEMGIYPA VDPLASTSRA LEPSIVGQEH 

       370        380        390        400        410        420 
YEVARDVQST LQKYRELQDI IAILGMDELS DEDKQTVERA RRIQFFLSQN FHVAEQFTGQ 

       430        440        450        460        470 
KGSYVPVKTT VANFKDILDG KYDHIPEDAF RLVGSMDDVI AKAKDMGVEV

« Hide

References

« Hide 'large scale' references
[1]"Whole genome sequencing of meticillin-resistant Staphylococcus aureus."
Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. expand/collapse author list , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.
Lancet 357:1225-1240(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: N315.
[2]"Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth."
Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.
J. Microbiol. Methods 60:247-257(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
Strain: N315.
[3]"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
Submitted (OCT-2007) to UniProtKB
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: N315.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000018 Genomic DNA. Translation: BAB43189.1.
PIRD90003.
RefSeqNP_375210.1. NC_002745.2.

3D structure databases

ProteinModelPortalP99112.
SMRP99112. Positions 1-467.
ModBaseSearch...

Protein-protein interaction databases

STRING158879.SA1905.

2D gel databases

SWISS-2DPAGEP99112.

Proteomic databases

PRIDEP99112.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB43189; BAB43189; BAB43189.
GeneID1124806.
KEGGsau:SA1905.
PATRIC19576268. VBIStaAur116463_2061.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0055.
HOGENOMHOG000009605.
KOK02112.
OMANHYDIAR.
ProtClustDBPRK09280.

Enzyme and pathway databases

BioCycSAUR158879:GJCB-2038-MONOMER.

Family and domain databases

Gene3D1.10.1140.10. 1 hit.
HAMAPMF_01347. ATP_synth_beta_bact.
InterProIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_a/bsu_N.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR024034. ATPase_F1_bsu/V1_C.
[Graphical view]
PANTHERPTHR15184:SF8. PTHR15184:SF8. 1 hit.
PfamPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF47917. ATPase_a/b_C. 1 hit.
SSF50615. ATPase_a/b_N. 1 hit.
TIGRFAMsTIGR01039. atpD. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameATPB_STAAN
AccessionPrimary (citable) accession number: P99112
Secondary accession number(s): Q99SF5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents