A1TD57

PR
Gene name
atpA
Protein name
ATP synthase subunit alpha
Names
ATP synthase F1 sector subunit alpha, F-ATPase subunit alpha
Species
Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii)
KEGG Pathway
mva:Mvan_4330
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)

470-548 (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 A1TD57

Entry ID Method Resolution Chain Position Source
AF-A1TD57-F1 Predicted AlphaFoldDB

No variants for A1TD57

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1TD57

No associated diseases with A1TD57

5 regional properties for A1TD57

Type Name Position InterPro Accession
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain 152 - 375 IPR000194
domain ATP synthase, alpha subunit, C-terminal 382 - 511 IPR000793
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain 29 - 95 IPR004100
active_site ATPase, alpha/beta subunit, nucleotide-binding domain, active site 366 - 375 IPR020003
domain ATP synthase, F1 complex, alpha subunit nucleotide-binding domain 97 - 378 IPR033732

Functions

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

2 GO annotations of cellular component

Name Definition
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
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.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAELTISASD IEGAIEDYVS SFTADSGREE IGVVIDAGDG IAHVEGLPSV MTQELLEFPG
70 80 90 100 110 120
GVLGVALNLD EHSVGAVILG EFEKIEQGQQ VKRTGEVLSV PVGDAFLGRV INPLGQPIDG
130 140 150 160 170 180
QGDIEAEGRR ALELQAPSVV QRQGVSEPLQ TGIKAIDSMT PIGRGQRQLI IGDRKTGKTA
190 200 210 220 230 240
VCVDTILNQR EAWATGDPKQ QVRCVYVAIG QKGTTIASVK RALEEGGAME CTTIVAAPAS
250 260 270 280 290 300
DAAGFKWLAP YTGSAIGQHW MYDGKHVLIV FDDLSKQADA YRAISLLLRR PPGREAFPGD
310 320 330 340 350 360
VFYLHSRLLE RCAKLSDELG GGSMTGLPII ETKANDISAF IPTNVISITD GQCFLESDLF
370 380 390 400 410 420
NQGVRPAINV GVSVSRVGGA AQIKAMKEVA GSLRLELSQY RELEAFAAFA SDLDAASKAQ
430 440 450 460 470 480
LDRGARLVEL LKQPQYTPYP VEDQVVAIYL GTGGHLDSVP VEDVARFESE LLEHVKASHG
490 500 510 520 530 540
DILAGIRESK KLSEEAEQKL ANVINEFKKG FSASDGSSVV VNEAEAEAMD EADVEKESVK
VRKPAPKK