Q982V5

PR
Gene name
clpX
Protein name
ATP-dependent Clp protease ATP-binding subunit ClpX
Names
Species
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) (Mesorhizobium loti (strain MAFF 303099))
KEGG Pathway
mlo:mlr8474
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

154-230 (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 Q982V5

Entry ID Method Resolution Chain Position Source
AF-Q982V5-F1 Predicted AlphaFoldDB

No variants for Q982V5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q982V5

No associated diseases with Q982V5

4 regional properties for Q982V5

Type Name Position InterPro Accession
domain AAA+ ATPase domain 112 - 332 IPR003593
domain ATPase, AAA-type, core 113 - 309 IPR003959
domain Zinc finger, ClpX C4-type 5 - 58 IPR010603
domain Clp ATPase, C-terminal 316 - 411 IPR019489

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

6 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
ATP-dependent protein folding chaperone Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis.
protein dimerization activity The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.
unfolded protein binding Binding to an unfolded protein.
zinc ion binding Binding to a zinc ion (Zn).

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
MSKVGNNSGD SKNTLYCSFC GKSQHEVRKL IAGPTVFICD ECVELCMDII REENKTSMVK
70 80 90 100 110 120
SREGVPTPQE ILKVLDDYVI GQPYAKRVLS VAVHNHYKRL AHAGKNNDVE LAKSNILLIG
130 140 150 160 170 180
PTGCGKTLLA QTLARIIDVP FTMADATTLT EAGYVGEDVE NIILKLLQSA DYNVERAQRG
190 200 210 220 230 240
IVYIDEIDKI SRKSDNPSIT RDVSGEGVQQ ALLKIMEGTV ASVPPQGGRK HPQQEFLQVD
250 260 270 280 290 300
TANILFICGG AFAGLDKIIS DRGRKTSIGF GATVASPEDR RTGDIFRQVE PEDLLKFGLI
310 320 330 340 350 360
PEFVGRLPVL ATLEDLDEPA LIQILTEPKN ALVKQYQRLF EMENVDLTFH ENALSAIAKR
370 380 390 400 410 420
AIERKTGARG LRSIMEAILL DTMFELPALE GVREVVISEE VVTGSARPLY IYSEQKEKKG
NVSA