Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q05825

Entry ID Method Resolution Chain Position Source
AF-Q05825-F1 Predicted AlphaFoldDB

No variants for Q05825

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q05825

No associated diseases with Q05825

4 regional properties for Q05825

Type Name Position InterPro Accession
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain 163 - 382 IPR000194
domain AAA+ ATPase domain 175 - 359 IPR003593
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain 40 - 106 IPR004100
active_site ATPase, alpha/beta subunit, nucleotide-binding domain, active site 373 - 382 IPR020003

Functions

Description
EC Number 7.1.2.2 Hydron translocation linked to the hydrolysis of a nucleoside triphosphate
Subcellular Localization
  • Mitochondrion
  • Mitochondrion inner membrane
  • Peripheral membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
mitochondrial proton-transporting ATP synthase complex A proton-transporting ATP synthase complex found in the mitochondrial membrane.
mitochondrial proton-transporting ATP synthase, catalytic core The hexamer, comprising three alpha and three beta subunits, that possesses the catalytic activity of the mitochondrial hydrogen-transporting ATP synthase.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
proton-transporting ATP synthase complex, catalytic core F(1) The sector of a hydrogen-transporting ATP synthase complex in which the catalytic activity resides; it comprises the catalytic core and central stalk, and is peripherally associated with a membrane, such as the plasma membrane or the mitochondrial inner membrane, when the entire ATP synthase is assembled.

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
proton-transporting ATP synthase activity, rotational mechanism Enables the synthesis of ATP from ADP and phosphate by the transfer of protons from one side of a membrane to the other by a rotational mechanism driven by a gradient according to the reaction: ADP + H2O + phosphate + H+(in) -> ATP + H+(out).
proton-transporting ATPase activity, rotational mechanism Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) = ADP + phosphate + H+(out), by a rotational mechanism.

2 GO annotations of biological process

Name Definition
proton motive force-driven ATP synthesis The transport of protons across a membrane to generate an electrochemical gradient (proton-motive force) that powers ATP synthesis.
proton motive force-driven mitochondrial ATP synthesis The transport of protons across a mitochondrial membrane to generate an electrochemical gradient (proton-motive force) that powers ATP synthesis.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P00829 ATP5F1B ATP synthase subunit beta, mitochondrial Bos taurus (Bovine) PR
Q5ZLC5 ATP5F1B ATP synthase subunit beta, mitochondrial Gallus gallus (Chicken) PR
P06576 ATP5F1B ATP synthase subunit beta, mitochondrial Homo sapiens (Human) PR
P56480 Atp5f1b ATP synthase subunit beta, mitochondrial Mus musculus (Mouse) PR
P10719 Atp5f1b ATP synthase subunit beta, mitochondrial Rattus norvegicus (Rat) PR
P46561 atp-2 ATP synthase subunit beta, mitochondrial Caenorhabditis elegans PR
10 20 30 40 50 60
MFALRAASKA DKNLLPFLGQ LSRSHAAKAA KAAAAANGKI VAVIGAVVDV QFDDNLPPIL
70 80 90 100 110 120
NALEVDNRSP RLVLEVAQHL GENTVRTIAM DGTEGLVRGQ KVLDTGYPIR IPVGAETLGR
130 140 150 160 170 180
IINVIGEPID ERGPIDTDKT AAIHAEAPEF VQMSVEQEIL VTGIKVVDLL APYAKGGKIG
190 200 210 220 230 240
LFGGAGVGKT VLIMELINNV AKAHGGYSVF AGVGERTREG NDLYNEMIEG GVISLKDKTS
250 260 270 280 290 300
KVALVYGQMN EPPGARARVA LTGLTVAEYF RDQEGQDVLL FIDNIFRFTQ AGSEVSALLG
310 320 330 340 350 360
RIPSAVGYQP TLATDMGSMQ ERITTTKKGS ITSVQAIYVP ADDLTDPAPA TTFAHLDATT
370 380 390 400 410 420
VLSRAIAELG IYPAVDPLDS TSRIMDPNII GQEHYNVARG VQKILQDYKS LQDIIAILGM
430 440 450 460 470 480
DELSEEDKLT VARARKIQRF LSQPFQVAEV FTGHAGKLVP LEQTIKGFSA ILAGDYDHLP
490 500
EVAFYMVGPI EEVVEKADRL AKEAA