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Protein

ATP synthase subunit beta, chloroplastic

Gene

atpB

Organism
Spinacia oleracea (Spinach)
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.

Catalytic activityi

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi172 – 1798ATPUniRule 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

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
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

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

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2366567.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 498498ATP synthase subunit beta, chloroplasticPRO_0000144550Add
BLAST

Proteomic databases

PRIDEiP00825.

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

MINTiMINT-147572.

Structurei

Secondary structure

1
498
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi21 – 277Combined sources
Beta strandi30 – 345Combined sources
Beta strandi46 – 494Combined sources
Beta strandi53 – 564Combined sources
Beta strandi62 – 676Combined sources
Beta strandi70 – 723Combined sources
Beta strandi74 – 807Combined sources
Beta strandi90 – 934Combined sources
Beta strandi95 – 973Combined sources
Beta strandi99 – 1046Combined sources
Turni105 – 1084Combined sources
Beta strandi119 – 1224Combined sources
Beta strandi127 – 1326Combined sources
Helixi139 – 1413Combined sources
Helixi156 – 1594Combined sources
Beta strandi168 – 1725Combined sources
Beta strandi174 – 1774Combined sources
Helixi178 – 18811Combined sources
Turni189 – 1924Combined sources
Beta strandi197 – 2037Combined sources
Helixi207 – 21812Combined sources
Beta strandi232 – 2376Combined sources
Helixi243 – 2464Combined sources
Helixi249 – 2557Combined sources
Helixi257 – 2604Combined sources
Turni261 – 2633Combined sources
Beta strandi267 – 2737Combined sources
Helixi276 – 28914Combined sources
Helixi295 – 2973Combined sources
Helixi302 – 3087Combined sources
Beta strandi310 – 3145Combined sources
Beta strandi324 – 3285Combined sources
Helixi330 – 3323Combined sources
Beta strandi334 – 3363Combined sources
Helixi337 – 3426Combined sources
Helixi343 – 3453Combined sources
Beta strandi347 – 3526Combined sources
Turni355 – 3606Combined sources
Beta strandi367 – 3693Combined sources
Turni377 – 3793Combined sources
Helixi382 – 40827Combined sources
Turni415 – 4173Combined sources
Helixi418 – 43013Combined sources
Turni439 – 4413Combined sources
Helixi451 – 4599Combined sources
Turni460 – 4667Combined sources
Beta strandi467 – 4693Combined sources
Helixi471 – 4733Combined sources
Turni474 – 4763Combined sources
Beta strandi478 – 4803Combined sources
Helixi481 – 4833Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FX0X-ray3.20B1-498[»]
1KMHX-ray3.40B1-498[»]
ProteinModelPortaliP00825.
SMRiP00825. Positions 19-485.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00825.

Family & Domainsi

Sequence similaritiesi

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

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.

P00825-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRINPTTSDP GVSTLEKKNL GRIAQIIGPV LDVAFPPGKM PNIYNALIVK
60 70 80 90 100
GRDTAGQPMN VTCEVQQLLG NNRVRAVAMS ATDGLTRGME VIDTGAPLSV
110 120 130 140 150
PVGGATLGRI FNVLGEPVDN LGPVDTRTTS PIHRSAPAFT QLDTKLSIFE
160 170 180 190 200
TGIKVVDLLA PYRRGGKIGL FGGAGVGKTV LIMELINNIA KAHGGVSVFG
210 220 230 240 250
GVGERTREGN DLYMEMKESG VINEQNIAES KVALVYGQMN EPPGARMRVG
260 270 280 290 300
LTALTMAEYF RDVNEQDVLL FIDNIFRFVQ AGSEVSALLG RMPSAVGYQP
310 320 330 340 350
TLSTEMGSLQ ERITSTKEGS ITSIQAVYVP ADDLTDPAPA TTFAHLDATT
360 370 380 390 400
VLSRGLAAKG IYPAVDPLDS TSTMLQPRIV GEEHYEIAQR VKETLQRYKE
410 420 430 440 450
LQDIIAILGL DELSEEDRLT VARARKIERF LSQPFFVAEV FTGSPGKYVG
460 470 480 490
LAETIRGFQL ILSGELDSLP EQAFYLVGNI DEATAKAMNL EMESKLKK
Length:498
Mass (Da):53,745
Last modified:October 1, 1996 - v2
Checksum:i77C8E00EF4B667F6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321D → N in AAA84626 (PubMed:16593238).Curated
Sequence conflicti105 – 1051A → P in AAA84626 (PubMed:16593238).Curated
Sequence conflicti122 – 1221G → R in AAA84626 (PubMed:16593238).Curated
Sequence conflicti157 – 1571D → N in AAA84626 (PubMed:16593238).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01441 Genomic DNA. Translation: AAA84626.1.
U23082 Genomic DNA. Translation: AAB60294.1.
AF528861 Genomic DNA. Translation: AAQ09249.1.
AJ400848 Genomic DNA. Translation: CAB88736.1.
PIRiA01028. PWSPB.
RefSeqiNP_054943.1. NC_002202.1.

Genome annotation databases

GeneIDi2715576.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01441 Genomic DNA. Translation: AAA84626.1.
U23082 Genomic DNA. Translation: AAB60294.1.
AF528861 Genomic DNA. Translation: AAQ09249.1.
AJ400848 Genomic DNA. Translation: CAB88736.1.
PIRiA01028. PWSPB.
RefSeqiNP_054943.1. NC_002202.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FX0X-ray3.20B1-498[»]
1KMHX-ray3.40B1-498[»]
ProteinModelPortaliP00825.
SMRiP00825. Positions 19-485.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-147572.

Chemistry

ChEMBLiCHEMBL2366567.

Proteomic databases

PRIDEiP00825.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2715576.

Miscellaneous databases

EvolutionaryTraceiP00825.
PROiP00825.

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. "Structures of the genes for the beta and epsilon subunits of spinach chloroplast ATPase indicate a dicistronic mRNA and an overlapping translation stop/start signal."
    Zurawski G., Bottomley W., Whitfeld P.R.
    Proc. Natl. Acad. Sci. U.S.A. 79:6260-6264(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Over-expression and refolding of beta-subunit from the chloroplast ATP synthase."
    Chen Z., Wu I., Richter M.L., Gegenheimer P.
    FEBS Lett. 298:69-73(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Parsing out signal and noise for seed-plant phylogenetic inference."
    Graham S.W., Rai H.S., Ikegami K., Reeves P.A., Olmstead R.G.
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide sequence and gene organization."
    Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G., Mache R.
    Plant Mol. Biol. 45:307-315(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Geant d'hiver and cv. Monatol.
  5. "Photolabeling of the phosphate binding site of chloroplast coupling factor 1 with [32P]azidonitrophenyl phosphate."
    Michel L., Garin J., Girault G., Vignais P.V.
    FEBS Lett. 313:90-93(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 313-354.
  6. "Inactivation of chloroplast H(+)-ATPase by modification of Lys beta 359, Lys alpha 176 and Lys alpha 266."
    Horbach M., Meyer H.E., Bickel-Sandkoetter S.
    Eur. J. Biochem. 200:449-456(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. "The structure of the chloroplast F1-ATPase at 3.2 A resolution."
    Groth G., Pohl E.
    J. Biol. Chem. 276:1345-1352(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 19-485 IN COMPLEX WITH ALPHA CHAIN.

Entry informationi

Entry nameiATPB_SPIOL
AccessioniPrimary (citable) accession number: P00825
Secondary accession number(s): Q6EYW8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.