Q65GJ4

PR
Gene name
clpX
Protein name
ATP-dependent Clp protease ATP-binding subunit ClpX
Names
Species
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46)
KEGG Pathway
bli:BL00619
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

19-97 (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 Q65GJ4

Entry ID Method Resolution Chain Position Source
AF-Q65GJ4-F1 Predicted AlphaFoldDB

No variants for Q65GJ4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q65GJ4

No associated diseases with Q65GJ4

4 regional properties for Q65GJ4

Type Name Position InterPro Accession
domain AAA+ ATPase domain 112 - 264 IPR003593
domain ATPase, AAA-type, core 113 - 310 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
MFKFNEEKGQ LKCSFCGKTQ DQVRKLVAGP GVYICDECIE LCTEIVEEEL GSEEEVEFKD
70 80 90 100 110 120
VPKPKEIREI LDEYVIGQDQ AKKSLAVAVY NHYKRINSNS KVDDVELSKS NISMIGPTGS
130 140 150 160 170 180
GKTLLAQTLA RILNVPFAIA DATSLTEAGY VGEDVENILL KLIQAADYDV EKAEKGIIYI
190 200 210 220 230 240
DEIDKVARKS ENPSITRDVS GEGVQQALLK ILEGTVASVP PQGGRKHPHQ EFIQIDTTNI
250 260 270 280 290 300
LFICGGAFDG IEQIIKRRLG QKVIGFGSDN KHEDLEKEAL LSKVLPEDLL RFGLIPEFIG
310 320 330 340 350 360
RLPIIASLEP LDEKALVEIL TKPKNALVKQ YRKMLELDDV ELVFEDEALT EIAKKAIERK
370 380 390 400 410 420
TGARGLRSII EGIMLDVMFD LPSREDIEKC VITGKTVTDG EPPRLIMKDG TVVNKDKKTS
A