ATP synthase subunit alpha 2 - Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)

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Q2T873 (ATPA2_BURTA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
ATP synthase subunit alpha 2
EC=3.6.3.14

Alternative name(s):
ATP synthase F1 sector subunit alpha 2
F-ATPase subunit alpha 2

Gene names

Name:	atpA2
Synonyms:	atpA-2
Ordered Locus Names:	BTH_II0426

Organism

Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]

Taxonomic identifier

271848 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	556 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit By similarity. HAMAP MF_01346
Catalytic activity	ATP + H₂O + H⁺(In) = ADP + phosphate + H⁺(Out). HAMAP MF_01346
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 inner membrane; Peripheral membrane protein By similarity HAMAP MF_01346.
Sequence similarities	Belongs to the ATPase alpha/beta chains family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Cell inner membrane Cell membrane Membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell proton-transporting ATP synthase complex, catalytic core F(1) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 556

556

ATP synthase subunit alpha 2 HAMAP MF_01346

PRO_0000238225

Regions

Nucleotide binding

177 – 184

ATP By similarity

Sites

Site

370

Required for activity By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q2T873 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 0201DE675E1F2C47
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FASTA

556

58,506

        10         20         30         40         50         60 
MTQTPDATGA AADARWLARR RGALACVALA PVAQALGRVE RVADGIAFVS GLEDAMLNEV 

        70         80         90        100        110        120 
LRFDGGVTGF AHTLDEDLIS VVLLDPDAGV QAQTAVTRTG AVLEVPVGPQ LLGRVVDPLG 

       130        140        150        160        170        180 
RPLDGGAPLG TADTLPIERP APEIIERDLV SEPLDTGVLI VDALFTIGRG QRELIIGDRA 

       190        200        210        220        230        240 
TGKTSLAIDA IVNQRHSDVI CVYVAIGQRA SAVRRVIDAV RRYGAPERCI FVVAPAACAP 

       250        260        270        280        290        300 
GLQWIAPFAG FSVAEYFRDR GQHALVVVDD LTKHAATHRE LALLTREPPG REAYPGDIFY 

       310        320        330        340        350        360 
VHARLLERAA KLSAKLGGGS LSALPIAETD AGNLAAYIPT NLISITDGQI VLDSALFAAN 

       370        380        390        400        410        420 
QRPAVDVGLS VSRVGGKAQH PALRAASGRL RLDYAQFLEL EAFTRFGGLT DARLRAQITR 

       430        440        450        460        470        480 
GERIRALITQ PRFRALRTLD EVVLLKALAA GVLDAMSPDL VAPLRERLPS WLDARLAPPR 

       490        500        510        520        530        540 
DRLADDAALS MLAESIGELV ERVAADAAHR AAAGGHAEDA ADDMGGALDG EHASGDATSI 

       550 
APTPPGGAEA GAPRKR

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References

[1]

"Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies."
Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D.
BMC Genomics 6:174-174(2005) [PubMed: 16336651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000085 Genomic DNA. Translation: ABC36034.1.
RefSeq	YP_438626.1. NC_007650.1.
3D structure databases
ProteinModelPortal	Q2T873.
SMR	Q2T873. Positions 34-475.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2T873.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3845697.
GenomeReviews	Gene locus BTH_II0426 in contig CP000085_GR.
KEGG	bte:BTH_II0426.
PATRIC	19298304. VBIBurTha36512_0483.
TIGR	BTH_II0426.
Phylogenomic databases
eggNOG	COG0056.
HOGENOM	HBG565875.
OMA	NVLCVYC.
ProtClustDB	PRK13343.
Enzyme and pathway databases
BioCyc	BTHA271848:BTH_II0426-MONOMER.
Family and domain databases
HAMAP	MF_01346. ATP_synth_alpha_bact. [Tree]
InterPro	IPR020003. ATPase_a/bsu_AS. IPR005294. ATPase_F1-cplx_asu. IPR018118. ATPase_F1/A1-cplx_a/bsu_N. IPR023366. ATPase_F1/A1-cplx_a_su_N. IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C. IPR004100. ATPase_F1/V1/A1-cplx_a/bsu_N. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. [Graphical view]
Gene3D	G3DSA:2.40.30.20. G3DSA:2.40.30.20. 1 hit.
KO	K02111.
PANTHER	PTHR15184:SF3. ATPase_F1_a. 1 hit.
Pfam	PF00006. ATP-synt_ab. 1 hit. PF00306. ATP-synt_ab_C. 1 hit. PF02874. ATP-synt_ab_N. 1 hit. [Graphical view]
SUPFAM	SSF47917. ATPase_a/b_C. 1 hit. SSF50615. ATPase_a/b_N. 1 hit.
TIGRFAMs	TIGR00962. AtpA. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPA2_BURTA

Accession

Primary (citable) accession number: Q2T873

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	January 24, 2006
Last modified:	January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents