ATP synthase subunit beta, chloroplastic - Arabidopsis thaliana (Mouse-ear cress)

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P19366 (ATPB_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 110. History...

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

Documents (2) |

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 beta, chloroplastic
EC=3.6.3.14

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

Gene names

Name:	atpB
Ordered Locus Names:	AtCg00480

Encoded on

Plastid; Chloroplast

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	498 AA.
Sequence status	Complete.
Protein existence	Evidence 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 MF_01347
Catalytic activity	ATP + H₂O + H⁺(In) = ADP + phosphate + H⁺(Out). HAMAP 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 four main subunits: a₁, b₁, b'₁ and c(9-12) By similarity.
Subcellular location	Plastid › chloroplast thylakoid membrane; Peripheral membrane protein By similarity HAMAP MF_01347.
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) Chloroplast Membrane Plastid Thylakoid
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference 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	chloroplast thylakoid 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 hydrogen-exporting ATPase activity, phosphorylative 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 – 498

498

ATP synthase subunit beta, chloroplastic HAMAP MF_01347

PRO_0000144496

Regions

Nucleotide binding

172 – 179

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.3

Modified residue

Phosphoserine Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P19366 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 174F4B075E7D57E3
Show »

FASTA

498

53,934

        10         20         30         40         50         60 
MRTNPTTSNP EVSIREKKNL GRIAQIIGPV LDVAFPPGKM PNIYNALVVK GRDTLGQEIN 

        70         80         90        100        110        120 
VTCEVQQLLG NNRVRAVAMS ATEGLKRGMD VVDMGNPLSV PVGGATLGRI FNVLGEPVDN 

       130        140        150        160        170        180 
LGPVDTRTTS PIHKSAPAFI ELDTKLSIFE TGIKVVDLLA PYRRGGKIGL FGGAGVGKTV 

       190        200        210        220        230        240 
LIMELINNIA KAHGGVSVFG GVGERTREGN DLYMEMKESG VINEQNLAES KVALVYGQMN 

       250        260        270        280        290        300 
EPPGARMRVG LTALTMAEYF RDVNEQDVLL FIDNIFRFVQ AGSEVSALLG RMPSAVGYQP 

       310        320        330        340        350        360 
TLSTEMGTLQ ERITSTKKGS ITSIQAVYVP ADDLTDPAPA TTFAHLDATT VLSRGLAAKG 

       370        380        390        400        410        420 
IYPAVDPLDS TSTMLQPRIV GEEHYETAQQ VKQTLQRYKE LQDIIAILGL DELSEEDRLT 

       430        440        450        460        470        480 
VARARKIERF LSQPFFVAEV FTGSPGKYVG LAETIRGFNL ILSGEFDSLP EQAFYLVGNI 

       490 
DEATAKATNL EMESKLKK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete structure of the chloroplast genome of Arabidopsis thaliana." Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S. DNA Res. 6:283-290(1999) [PubMed: 10574454] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Nucleotide sequence of chloroplast CF1-ATPase epsilon-subunit and elongator tRNAMet genes from Arabidopsis thaliana." Chen H.-C., Wintz H., Weil J.-H., Pillay D.T.N. Nucleic Acids Res. 16:10372-10372(1988) [PubMed: 2904134] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 486-498. Strain: cv. Landsberg erecta.
[3]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-13, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP000423 Genomic DNA. Translation: BAA84392.1. X12889 Genomic DNA. Translation: CAA31380.1.
IPI	IPI00525776.
PIR	S01904.
RefSeq	NP_051066.1. NC_000932.1.
3D structure databases
ProteinModelPortal	P19366.
SMR	P19366. Positions 19-485.
ModBase	Search...
Protein-protein interaction databases
IntAct	P19366. 1 interaction.
STRING	P19366.
2D gel databases
SWISS-2DPAGE	P19366.
Proteomic databases
PRIDE	P19366.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	ATCG00480.1; ATCG00480.1; ATCG00480.
GeneID	844757.
GenomeReviews	Gene locus ATCG00480 in contig AP000423_GR.
KEGG	ath:ArthCp029.
NMPDR	fig\|3702.1.peg.28.
Organism-specific databases
TAIR	AtCg00480.
Phylogenomic databases
HOGENOM	HBG565875.
PhylomeDB	P19366.
ProtClustDB	CHL00060.
Gene expression databases
Genevestigator	P19366.
GermOnline	ATCG00480. Arabidopsis thaliana.
Family and domain databases
HAMAP	MF_01347. ATP_synth_beta_bact. [Tree]
InterPro	IPR020003. ATPase_a/bsu_AS. IPR003593. ATPase_AAA+_core. IPR005722. ATPase_F1-cplx_bsu. IPR018118. ATPase_F1/A1-cplx_a/bsu_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. IPR024034. ATPase_F1_bsu/V1_C. [Graphical view]
Gene3D	G3DSA:1.10.1140.10. G3DSA:1.10.1140.10. 1 hit.
KO	K02112.
Pfam	PF00006. ATP-synt_ab. 1 hit. PF00306. ATP-synt_ab_C. 1 hit. PF02874. ATP-synt_ab_N. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. [Graphical view]
SUPFAM	SSF47917. ATPase_a/b_C. 1 hit. SSF50615. ATPase_a/b_N. 1 hit.
TIGRFAMs	TIGR01039. AtpD. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPB_ARATH

Accession

Primary (citable) accession number: P19366

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	May 30, 2000
Last modified:	November 16, 2011
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

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

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents