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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)DescriptionActionsGraphical viewLength
Nucleotide bindingi172 – 179ATPUniRule annotation8

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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesChenopodiaceaeChenopodioideaeAnserineaeSpinacia

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 databases

ChEMBLiCHEMBL2366567.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001445501 – 498ATP synthase subunit beta, chloroplasticAdd BLAST498

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

1498
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi21 – 27Combined sources7
Beta strandi30 – 34Combined sources5
Beta strandi46 – 49Combined sources4
Beta strandi53 – 56Combined sources4
Beta strandi62 – 67Combined sources6
Beta strandi70 – 72Combined sources3
Beta strandi74 – 80Combined sources7
Beta strandi90 – 93Combined sources4
Beta strandi95 – 97Combined sources3
Beta strandi99 – 104Combined sources6
Turni105 – 108Combined sources4
Beta strandi119 – 122Combined sources4
Beta strandi127 – 132Combined sources6
Helixi139 – 141Combined sources3
Helixi156 – 159Combined sources4
Beta strandi168 – 172Combined sources5
Beta strandi174 – 177Combined sources4
Helixi178 – 188Combined sources11
Turni189 – 192Combined sources4
Beta strandi197 – 203Combined sources7
Helixi207 – 218Combined sources12
Beta strandi232 – 237Combined sources6
Helixi243 – 246Combined sources4
Helixi249 – 255Combined sources7
Helixi257 – 260Combined sources4
Turni261 – 263Combined sources3
Beta strandi267 – 273Combined sources7
Helixi276 – 289Combined sources14
Helixi295 – 297Combined sources3
Helixi302 – 308Combined sources7
Beta strandi310 – 314Combined sources5
Beta strandi324 – 328Combined sources5
Helixi330 – 332Combined sources3
Beta strandi334 – 336Combined sources3
Helixi337 – 342Combined sources6
Helixi343 – 345Combined sources3
Beta strandi347 – 352Combined sources6
Turni355 – 360Combined sources6
Beta strandi367 – 369Combined sources3
Turni377 – 379Combined sources3
Helixi382 – 408Combined sources27
Turni415 – 417Combined sources3
Helixi418 – 430Combined sources13
Turni439 – 441Combined sources3
Helixi451 – 459Combined sources9
Turni460 – 466Combined sources7
Beta strandi467 – 469Combined sources3
Helixi471 – 473Combined sources3
Turni474 – 476Combined sources3
Beta strandi478 – 480Combined sources3
Helixi481 – 483Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FX0X-ray3.20B1-498[»]
1KMHX-ray3.40B1-498[»]
ProteinModelPortaliP00825.
SMRiP00825.
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. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR005722. ATP_synth_F1_bsu.
IPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_F1/V1/A1_a/bsu_N.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR024034. ATPase_F1/V1_bsu_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]
SUPFAMiSSF50615. 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)DescriptionActionsGraphical viewLength
Sequence conflicti32D → N in AAA84626 (PubMed:16593238).Curated1
Sequence conflicti105A → P in AAA84626 (PubMed:16593238).Curated1
Sequence conflicti122G → R in AAA84626 (PubMed:16593238).Curated1
Sequence conflicti157D → N in AAA84626 (PubMed:16593238).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FX0X-ray3.20B1-498[»]
1KMHX-ray3.40B1-498[»]
ProteinModelPortaliP00825.
SMRiP00825.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-147572.

Chemistry databases

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. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR005722. ATP_synth_F1_bsu.
IPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_F1/V1/A1_a/bsu_N.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR024034. ATPase_F1/V1_bsu_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]
SUPFAMiSSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 135 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.