ATP synthase subunit alpha 2 - Burkholderia pseudomallei

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Reviewed, UniProtKB/Swiss-Prot Q63IX0 (ATPA2_BURPS)

Last modified November 3, 2009. Version 42. History...

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

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    ATP synthase subunit alpha 2
    EC=3.6.3.14
Alternative name(s):
    F-ATPase subunit alpha 2
    ATP synthase F1 sector subunit alpha 2

Gene names

Name:	atpA2
Ordered Locus Names:	BPSS1946

Organism

Burkholderia pseudomallei (Pseudomonas pseudomallei) [Complete proteome] [HAMAP]

Taxonomic identifier

28450 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	666 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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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.
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.
Sequence similarities	Belongs to the ATPase alpha/beta chains family.

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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	plasma membrane ATP synthesis coupled proton transport Inferred from electronic annotation. Source: HAMAP
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW 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: HAMAP hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: HAMAP proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 666

666

ATP synthase subunit alpha 2 HAMAP MF_01346

PRO_0000238220

Regions

Nucleotide binding

182 – 189

ATP By similarity

Sites

Site

375

Required for activity By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q63IX0-1 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: ACE4F3CFA1E4193E
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FASTA

666

69,788

        10         20         30         40         50         60 
MTPTPDAPAA AAADAATGAG WLARRRGALA RVALAPVAQA IGRVERVADG IAFVSGLEDT 

        70         80         90        100        110        120 
MLNEVLRFEG GVTGFAHTLD EDLISVVLLD PDAGVRAQTA VARTGAVLEV PAGPQLLGRV 

       130        140        150        160        170        180 
VDPLGRPLDG GAPLDAAHTL PIERAAPAII ERDLVSEPLD TGVLIVDALF TIGRGQRELI 

       190        200        210        220        230        240 
IGDRATGKTS LAIDAIVNQR HSDVICVYVA IGQRASAVRR VIDAVRRYGA PERCVFVVAP 

       250        260        270        280        290        300 
AACAPGLQWI APFAGFSIAE YFRDRGQHAL VVVDDLTKHA ATHRELALLT REPPGREAYP 

       310        320        330        340        350        360 
GDIFYVHARL LERAAKLSAA LGGGSLSALP IAETDAGNLA AYIPTNLISI TDGQIVLDSA 

       370        380        390        400        410        420 
LFAANQRPAV DVGLSVSRVG GKAQHPALRA ASGRLRLDYA QFLELEAFTR FGGLTDARLR 

       430        440        450        460        470        480 
AQITRGERIR ALITQPRFRA LRTLDEVVLL KALAAGALDA MSPDLVAPLR ERLPAWLDAR 

       490        500        510        520        530        540 
IAALTPALAP PRDWLADDAA LDALAESVGE LIERIAADAA RRATAGMPAE DAAGDIGGAF 

       550        560        570        580        590        600 
GGEQARGDAD RDADHGANRE VSREVSPEAS REVSREVSCE VSHEADRDAA ADAARVAGRA 

       610        620        630        640        650        660 
PGRAEPDRAA PRAMPDGPPR AQADGDRASA SRPRPDARGD AARTAPSPQG GADANVDAEA 


EARHKR

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References

[1]

"Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei."
Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F., Challis G.L.

Parkhill J.
Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004) [PubMed: 15377794] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K96243.

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Cross-references

Sequence databases
	BX571966 Genomic DNA. Translation: CAH39424.1.
RefSeq	YP_111952.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3096069.
GenomeReviews	Gene locus BPSS1946 in contig BX571966_GR.
KEGG	bps:BPSS1946.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q63IX0.
OMA	NVLCVYC.
Enzyme and pathway databases
BioCyc	BPSE272560:BPSS1946-MON.
BRENDA	3.6.3.14. 275934.
Family and domain databases
HAMAP	MF_01346. [Tree]
InterPro	IPR005294. ATPase_F1-cplx_asu. IPR017458. ATPase_F1-cplx_asu_C. IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C. IPR004100. ATPase_F1/V1/A1-cplx_a/bsu_N. IPR020003. ATPase_F1/V1/A1_a/bsu_AS. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. [Graphical view]
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]
TIGRFAMs	TIGR00962. atpA. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

ATPA2_BURPS

Accession

Primary (citable) accession number: Q63IX0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	October 25, 2004
Last modified:	November 3, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

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

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents