B7J127

PR
Gene name
atpA
Protein name
V-type ATP synthase alpha chain
Names
V-ATPase subunit A
Species
Borreliella burgdorferi (strain ZS7) (Borrelia burgdorferi)
KEGG Pathway
bbz:BbuZS7_0094
EC number
7.1.2.2: Hydron translocation linked to the hydrolysis of a nucleoside triphosphate
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

365-434 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for B7J127

Entry ID Method Resolution Chain Position Source
AF-B7J127-F1 Predicted AlphaFoldDB

No variants for B7J127

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B7J127

No associated diseases with B7J127

3 regional properties for B7J127

Type Name Position InterPro Accession
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain 220 - 439 IPR000194
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain 7 - 70 IPR004100
domain ATPsynthase alpha/beta subunit, N-terminal extension 87 - 209 IPR031686

Functions

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

1 GO annotations of cellular component

Name Definition
proton-transporting ATP synthase complex A proton-transporting two-sector ATPase complex that catalyzes the phosphorylation of ADP to ATP during oxidative phosphorylation. The complex comprises a membrane sector (F0) that carries out proton transport and a cytoplasmic compartment sector (F1) that catalyzes ATP synthesis by a rotational mechanism; the extramembrane sector (containing 3 a and 3 b subunits) is connected via the d-subunit to the membrane sector by several smaller subunits. Within this complex, the g and e subunits and the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis. This movement is driven by the hydrogen ion electrochemical potential gradient.

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
MNTKGKVVGV NGNLVTIEVE GSVFMNEVLF VKTAGRNLKA EVIRIRGNEV DAQVFELTKG
70 80 90 100 110 120
ISVGDLVEFT DKLLTVELGP GLLTQVYDGL QNPLPELAIQ CGFFLERGVY LRPLNKDKKW
130 140 150 160 170 180
NFKKTSKVGD IVIAGDFLGF VIEGTVHHQI MIPFYKRDSY KIVEIVSDGD YSIDEQIAVI
190 200 210 220 230 240
EDDSGMRHNI TMSFHWPVKV PITNYKERLI PSEPMLTQTR IIDTFFPVAK GGTFCIPGPF
250 260 270 280 290 300
GAGKTVLQQV TSRNADVDVV IIAACGERAG EVVETLKEFP ELMDPKTGKS LMDRTCIICN
310 320 330 340 350 360
TSSMPVAARE ASVYTAITIG EYYRQMGLDI LLLADSTSRW AQAMREMSGR LEEIPGEEAF
370 380 390 400 410 420
PAYLESVIAS FYERAGIVVL NNGDIGSVTV GGSVSPAGGN FEEPVTQATL KVVGAFHGLT
430 440 450 460 470 480
RERSDARKFP AISPLESWSK YKGVIDQKKT EYARSFLVKG NEINQMMKVV GEEGISNDDF
490 500 510 520 530 540
LIYLKSELLD SCYLQQNSFD SIDAAVSSER QNYMFDIVYN ILKTNFEFSD KLQARDFINE
550 560 570
LRQNLLDMNL SSFKDHKFNK LEHALGELIN FKKVI