Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

ATP synthase subunit beta, mitochondrial

Gene

atp-2

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Required during male mating behavior for the response to hermaphrodite contact, acting with lov-1 and pkd-2. May be involved in polycystin signaling.1 Publication

Catalytic activityi

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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi215 – 222ATPSequence analysis8

GO - Molecular functioni

GO - Biological processi

  • ATP synthesis coupled proton transport Source: InterPro
  • dauer larval development Source: WormBase
  • defecation Source: WormBase
  • defense response to Gram-negative bacterium Source: UniProtKB
  • determination of adult lifespan Source: WormBase
  • embryonic morphogenesis Source: WormBase
  • gonad development Source: WormBase
  • inductive cell migration Source: WormBase
  • mating behavior Source: WormBase
  • negative regulation of gene expression Source: UniProtKB
  • nematode larval development Source: WormBase
  • pharyngeal pumping Source: WormBase

Keywordsi

Molecular functionHydrolase
Biological processATP synthesis, Behavior, Hydrogen ion transport, Ion transport, Transport
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit beta, mitochondrial (EC:3.6.3.14)
Gene namesi
Name:atp-2
ORF Names:C34E10.6
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiC34E10.6 ; CE29950 ; WBGene00000229 ; atp-2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell projection, CF(1), Cilium, Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000002450? – 538ATP synthase subunit beta, mitochondrial
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

EPDiP46561
PaxDbiP46561
PeptideAtlasiP46561
PRIDEiP46561

Expressioni

Tissue specificityi

Expressed in three categories of adult male sensory neurons: tail ray B neurons, HOB hook neuron and head cephalic (CEM) neurons.1 Publication

Developmental stagei

Widely expressed throughout development in both males and hermaphrodites.

Gene expression databases

BgeeiWBGene00000229

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 three main subunits: a, b and c. Interacts (via N-terminus) with lov-1 (via PLAT domain).1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein domain specific binding Source: WormBase

Protein-protein interaction databases

BioGridi40947, 15 interactors
DIPiDIP-24363N
IntActiP46561, 15 interactors
STRINGi6239.C34E10.6.2

Structurei

3D structure databases

ProteinModelPortaliP46561
SMRiP46561
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1350 Eukaryota
COG0055 LUCA
GeneTreeiENSGT00550000074800
HOGENOMiHOG000009605
InParanoidiP46561
KOiK02133
OMAiFNMIMDG
OrthoDBiEOG091G0KVV
PhylomeDBiP46561

Family and domain databases

Gene3Di1.10.1140.10, 1 hit
HAMAPiMF_01347 ATP_synth_beta_bact, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR005722 ATP_synth_F1_bsu
IPR020003 ATPase_a/bsu_AS
IPR004100 ATPase_F1/V1/A1_a/bsu_N
IPR036121 ATPase_F1/V1/A1_a/bsu_N_sf
IPR000194 ATPase_F1/V1/A1_a/bsu_nucl-bd
IPR024034 ATPase_F1/V1_b/a_C
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF00006 ATP-synt_ab, 1 hit
PF02874 ATP-synt_ab_N, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SUPFAMiSSF50615 SSF50615, 1 hit
SSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR01039 atpD, 1 hit
PROSITEiView protein in PROSITE
PS00152 ATPASE_ALPHA_BETA, 1 hit

Sequencei

Sequence statusi: Complete.

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

P46561-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASRSLASIS RSASRLLQSN VQKCALPAAS IRLSSNNVES KKGIHTGVAT
60 70 80 90 100
QQAAAATKVS AKATAANASG RIVAVIGAVV DVQFDENLPP ILNGLEVVGR
110 120 130 140 150
SPRLILEVSQ HLGDNVVRCI AMDGTEGLVR GQPVADTGDP IKIPVGPETL
160 170 180 190 200
GRIMNVIGEP IDERGPIASK NFAAIHAEAP EFVEMSVEQE ILVTGIKVVD
210 220 230 240 250
LLAPYAKGGK IGLFGGAGVG KTVLIMELIN NVAKAHGGYS VFAGVGERTR
260 270 280 290 300
EGNDLYHEMI EGGVIDLKGK NSKVSLVYGQ MNEPPGARAR VCLTGLTVAE
310 320 330 340 350
YFRDQEGQDV LLFIDNIFRF TQAGSEVSAL LGRIPSAVGY QPTLATDMGS
360 370 380 390 400
MQERITTTKK GSITSVQAIY VPADDLTDPA PATTFAHLDA TTVLSRGIAE
410 420 430 440 450
LAIYPAVDPL DSTSRIMDPN VVGQNHYDIA RGVQKILQDY KSLQDIIAIL
460 470 480 490 500
GMDELSEEDK LTVSRARKIQ RFLSQPFQVA EVFTGHQGKF VSLEETIRGF
510 520 530
TMILKGELDH LPEVAFYMQG GIDDVFKKAE ELAKQHGN
Length:538
Mass (Da):57,527
Last modified:June 6, 2002 - v2
Checksum:i5B4D4A9C45D337D5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO080774 Genomic DNA Translation: CCD66650.1
PIRiT15763
RefSeqiNP_498111.2, NM_065710.5
UniGeneiCel.38639

Genome annotation databases

EnsemblMetazoaiC34E10.6.1; C34E10.6.1; WBGene00000229
C34E10.6.2; C34E10.6.2; WBGene00000229
C34E10.6.3; C34E10.6.3; WBGene00000229
GeneIDi175716
KEGGicel:CELE_C34E10.6
UCSCiC34E10.6.2 c. elegans

Similar proteinsi

Entry informationi

Entry nameiATPB_CAEEL
AccessioniPrimary (citable) accession number: P46561
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: June 6, 2002
Last modified: April 25, 2018
This is version 150 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health