ATP synthase subunit beta, chloroplastic - Chlamydomonas reinhardtii

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P06541 (ATPB_CHLRE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 108. 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 beta, chloroplastic
EC=3.6.3.14

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

Gene names

Name:

atpB

Encoded on

Plastid; Chloroplast

Organism

Chlamydomonas reinhardtii (Chlamydomonas smithii)

Taxonomic identifier

3055 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Chlorophyta › Chlorophyceae › Chlamydomonadales › Chlamydomonadaceae › Chlamydomonas

Protein attributes

Sequence length	481 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.
Sequence caution	The sequence AAA84146.1 differs from that shown. Reason: Erroneous initiation. The sequence ACJ50145.1 differs from that shown. Reason: Erroneous initiation. The sequence ACK37278.1 differs from that shown. Reason: Erroneous initiation. The sequence ACK37279.1 differs from that shown. Reason: Erroneous initiation. The sequence DAA00958.1 differs from that shown. Reason: Erroneous initiation.

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
Technical term	Complete proteome Direct protein sequencing 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

Initiator methionine

Removed Ref.3

Chain

2 – 481

480

ATP synthase subunit beta, chloroplastic HAMAP MF_01347

PRO_0000144505

Regions

Nucleotide binding

162 – 169

ATP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P06541 [UniParc].

Last modified March 24, 2009. Version 3.
Checksum: 448C50C9BAA93BF4
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FASTA

481

52,040

        10         20         30         40         50         60 
MSDSIETKNM GRIVQIIGPV LDIVFAKGQV PNIYNALTIR AKNSAGTEMA VTCEVQQLLG 

        70         80         90        100        110        120 
DNCVRAVSMN PTEGLMRGME VVDTGKPLSV PVGKVTLGRI FNVLGEPVDN MGNVKVEETL 

       130        140        150        160        170        180 
PIHRTAPAFV DLDTRLSIFE TGIKVVDLLA PYRRGGKIGL FGGAGVGKTV LIMELINNIA 

       190        200        210        220        230        240 
KAHGGVSVFA GVGERTREGN DLYTEMKESG VIVEKNLSDS KVALVYGQMN EPPGARMRVA 

       250        260        270        280        290        300 
LTALTMAEYF RDVNKQDVLF FIDNIFRFVQ AGAEVSALLG RMPSAVGYQP TLATEMGGLQ 

       310        320        330        340        350        360 
ERITSTKDGS ITSIQAVYVP ADDLTDPAPA TTFAHLDATT VLSRNLAAKG IYPAVDPLES 

       370        380        390        400        410        420 
TSTMLQPWIL GEKHYDSAQS VKKTLQRYKE LQDIIAILGL DELSEEDRLI VARARKIERF 

       430        440        450        460        470        480 
LSQPFFVAEV FTGSPGKYVS LAETIEGFGK IFAGELDDLP EQAFYLVGNI TEAISKAASL 


K

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sequence of the chloroplast atpB gene and its flanking regions in Chlamydomonas reinhardtii." Woessner J.P., Gillham N.W., Boynton J.E. Gene 44:17-28(1986) [PubMed: 2876928] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Nucleotide diversity in the chloroplast genome of Chlamydomonas reinhardtii." United States Department of Energy Joint Genome Institute Smith D.R. Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CC-2290 / S1 D2 and CC-503.
[3]	"Isolation of CF0CF1 from Chlamydomonas reinhardtii cw15 and the N-terminal amino acid sequences of the CF0CF1 subunits." Fiedler H.R., Schmid R., Leu S., Shavit N., Strotmann H. FEBS Lett. 377:163-166(1995) [PubMed: 8543042] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-20. Strain: cw15.
[4]	"The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a sea of repeats." Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H., Stern D.B. Plant Cell 14:2659-2679(2002) [PubMed: 12417694] [Abstract] Cited for: IDENTIFICATION, COMPLETE PLASTID GENOME.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M13704 Genomic DNA. Translation: AAA84146.1. Different initiation. FJ423446 Genomic DNA. Translation: ACJ50145.1. Different initiation. FJ436946 Genomic DNA. Translation: ACK37278.1. Different initiation. FJ436947 Genomic DNA. Translation: ACK37279.1. Different initiation. BK000554 Genomic DNA. Translation: DAA00958.1. Different initiation.
PIR	C24829.
RefSeq	NP_958414.1. NC_005353.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2717034.
KEGG	cre:ChreCp058.
Phylogenomic databases
ProtClustDB	CHL00060.
Enzyme and pathway databases
BioCyc	CHLAMY:CHRECP058-MONOMER.
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_CHLRE

Accession

Primary (citable) accession number: P06541
Secondary accession number(s): B7U1J8, Q9T2G7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	March 24, 2009
Last modified:	December 14, 2011
This is version 108 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant 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

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents