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 O83443

Entry ID Method Resolution Chain Position Source
AF-O83443-F1 Predicted AlphaFoldDB

No variants for O83443

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O83443

No associated diseases with O83443

No regional properties for O83443

Type Name Position InterPro Accession
No domain, repeats, and functional sites for O83443

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

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.

1 GO annotations of biological process

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

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAVRLTKNEL KRQKETLKTF RRFLPTLQLK KQQLYAEIRA VEARASEVRS RADALRQDVQ
70 80 90 100 110 120
QWVAVFSESG VFDARLLRVQ EVKKTYASIA GVRIPCFLEV HFACPPYDLY RVPLWVDTAV
130 140 150 160 170 180
RKMQEVLSLD LEAHVLDEQA LLLGAELRTT TQRVNLFEKV KIPETRACIR KITVYLGDQQ
190 200
VAAVVRGKMS KKNLVDVSRM EQEDTR