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Protein

ATP synthase subunit beta, chloroplastic

Gene

atpB

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.UniRule annotation

Catalytic activityi

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi162 – 1698ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciCHLAMY:CHRECP058-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit beta, chloroplasticUniRule annotation (EC:3.6.3.14UniRule annotation)
Alternative name(s):
ATP synthase F1 sector subunit betaUniRule annotation
F-ATPase subunit betaUniRule annotation
Gene namesi
Name:atpBUniRule annotation
Encoded oniPlastid; Chloroplast
OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifieri3055 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas
Proteomesi
  • UP000006906 Componenti: Chloroplast

Subcellular locationi

  • Plastidchloroplast thylakoid membrane UniRule annotation; Peripheral membrane protein UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CF(1), Chloroplast, Membrane, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 481480ATP synthase subunit beta, chloroplasticPRO_0000144505Add
BLAST

Proteomic databases

PaxDbiP06541.
PRIDEiP06541.

Interactioni

Subunit structurei

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).UniRule annotation

Protein-protein interaction databases

STRINGi3055.DAA00958.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.UniRule annotation

Phylogenomic databases

eggNOGiKOG1350. Eukaryota.
COG0055. LUCA.
InParanoidiP06541.
KOiK02112.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact.
InterProiIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06541-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDSIETKNM GRIVQIIGPV LDIVFAKGQV PNIYNALTIR AKNSAGTEMA
60 70 80 90 100
VTCEVQQLLG DNCVRAVSMN PTEGLMRGME VVDTGKPLSV PVGKVTLGRI
110 120 130 140 150
FNVLGEPVDN MGNVKVEETL PIHRTAPAFV DLDTRLSIFE TGIKVVDLLA
160 170 180 190 200
PYRRGGKIGL FGGAGVGKTV LIMELINNIA KAHGGVSVFA GVGERTREGN
210 220 230 240 250
DLYTEMKESG VIVEKNLSDS KVALVYGQMN EPPGARMRVA LTALTMAEYF
260 270 280 290 300
RDVNKQDVLF FIDNIFRFVQ AGAEVSALLG RMPSAVGYQP TLATEMGGLQ
310 320 330 340 350
ERITSTKDGS ITSIQAVYVP ADDLTDPAPA TTFAHLDATT VLSRNLAAKG
360 370 380 390 400
IYPAVDPLES TSTMLQPWIL GEKHYDSAQS VKKTLQRYKE LQDIIAILGL
410 420 430 440 450
DELSEEDRLI VARARKIERF LSQPFFVAEV FTGSPGKYVS LAETIEGFGK
460 470 480
IFAGELDDLP EQAFYLVGNI TEAISKAASL K
Length:481
Mass (Da):52,040
Last modified:March 24, 2009 - v3
Checksum:i448C50C9BAA93BF4
GO

Sequence cautioni

The sequence AAA84146.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence ACJ50145.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence ACK37278.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence ACK37279.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence DAA00958.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiC24829.
RefSeqiNP_958414.1. NC_005353.1.

Genome annotation databases

GeneIDi2717034.
KEGGicre:ChreCp058.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiC24829.
RefSeqiNP_958414.1. NC_005353.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3055.DAA00958.

Proteomic databases

PaxDbiP06541.
PRIDEiP06541.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2717034.
KEGGicre:ChreCp058.

Phylogenomic databases

eggNOGiKOG1350. Eukaryota.
COG0055. LUCA.
InParanoidiP06541.
KOiK02112.

Enzyme and pathway databases

BioCyciCHLAMY:CHRECP058-MONOMER.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact.
InterProiIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome: addressing the mutational-hazard hypothesis."
    Smith D.R., Lee R.W.
    BMC Evol. Biol. 9:120-120(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, COMPLETE PLASTID GENOME.

Entry informationi

Entry nameiATPB_CHLRE
AccessioniPrimary (citable) accession number: P06541
Secondary accession number(s): B7U1J8, Q9T2G7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: March 24, 2009
Last modified: May 11, 2016
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.