C1CES2

PR
Gene name
atpA
Protein name
V-type ATP synthase alpha chain
Names
V-ATPase subunit A
Species
Streptococcus pneumoniae (strain JJA)
KEGG Pathway
sjj:SPJ_1233
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)

70-144 (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 C1CES2

Entry ID Method Resolution Chain Position Source
AF-C1CES2-F1 Predicted AlphaFoldDB

No variants for C1CES2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C1CES2

No associated diseases with C1CES2

4 regional properties for C1CES2

Type Name Position InterPro Accession
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain 213 - 436 IPR000194
domain ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain 6 - 68 IPR004100
active_site ATPase, alpha/beta subunit, nucleotide-binding domain, active site 427 - 436 IPR020003
domain ATPsynthase alpha/beta subunit, N-terminal extension 84 - 204 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
MTQGKIIKVS GPLVIASGMQ EANIQDICRV GKLGLIGEII EMRRDQASIQ VYEETSGLGP
70 80 90 100 110 120
GEPVVTTGEP LSVELGPGLI SQMFDGIQRP LDRFKLATHN DFLVRGVEVP SLDRDIKWHF
130 140 150 160 170 180
DSTIAIGQKV STGDILGTVK ETEVVNHKIM VPYGVSGEVV SIASGDFTID EVVYEIKKLD
190 200 210 220 230 240
GSFYKGTLMQ KWPVRKARPV SKRLIPEEPL ITGQRVIDAF FPVTKGGAAA VPGPFGAGKT
250 260 270 280 290 300
VVQHQVAKFA NVDIVIYVGC GERGNEMTDV LNEFPELIDP NTGQSIMQRT VLIANTSNMP
310 320 330 340 350 360
VAAREASIYT GITMAEYFRD MGYSVAIMAD STSRWAEALR EMSGRLEEMP GDEGYPAYLG
370 380 390 400 410 420
SRIAEYYERA GRSQVLGLPE REGTITAIGA VSPPGGDISE PVTQNTLRIV KVFWGLDAPL
430 440 450 460 470 480
AQRRHFPAIN WLTSYSLYKD SVGTYIDGKE KTDWNSKITR AMNYLQRESS LEEIVRLVGI
490 500 510 520 530 540
DSLSDNERLT MEIAKQIRED YLQQNAFDSV DTFTSFAKQE AMLSNILTFA DQANHALELG
550 560 570 580 590
SYFTEIMEGT VAVRDRMARS KYVSEDRLDE IKIISNEITH QIHLILETGG L