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 B0K8E7

Entry ID Method Resolution Chain Position Source
AF-B0K8E7-F1 Predicted AlphaFoldDB

No variants for B0K8E7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B0K8E7

No associated diseases with B0K8E7

2 regional properties for B0K8E7

Type Name Position InterPro Accession
domain ATP synthase, F1 complex, delta/epsilon subunit, N-terminal 6 - 84 IPR020546
domain ATP synthase epsilon subunit, C-terminal domain 89 - 133 IPR020547

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

2 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).

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
MLREYKTVRE IVGPLMLVEK VEGVKYNELV EIETGTGEIR RGQVLEVNGD KALVQLFEGS
70 80 90 100 110 120
TGLNINDCKV RFVGKSIELG VSIDMLGRVF DGLGRPRDKG PMIIPEKRLD INGNPINPTA
130 140 150 160 170 180
RDYPSEFIQT GISAIDGLNT LVRGQKLPIF SGSGLPHAQL AAQIARQAKV LGSDSKFAVV
190 200 210 220 230 240
FAAMGITFEE ADYFISDFRR TGAIDRSVLF INLANDPAIE RIATPRMALT CAEFLAYEKE
250 260 270 280 290 300
MHVLVIMTDM TNYCEALREV SAARKEVPGR RGYPGYLYTD LATIYERAGR IKGRKGSITQ
310 320 330 340 350 360
IPILTMPEDD KTHPIPDLTG YITEGQIILS RDLYRKGIYP PIDVLPSLSR LKDKGIGQGK
370 380 390 400 410 420
TREDHADLMN QLFASYARGK QAKELAVILG EAALSDTDKL YAKFADEFEA RYVAQREDED
430 440 450
RSIEETLAIG WDLLTILPRA ELKRVRDEYI DKYLPEKGE