Q1AVS9

PR
Gene name
clpP
Protein name
ATP-dependent Clp protease proteolytic subunit
Names
Endopeptidase Clp
Species
Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1)
KEGG Pathway
rxy:Rxyl_1537
EC number
3.4.21.92: Serine endopeptidases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-48 (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 Q1AVS9

Entry ID Method Resolution Chain Position Source
AF-Q1AVS9-F1 Predicted AlphaFoldDB

No variants for Q1AVS9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q1AVS9

No associated diseases with Q1AVS9

9 regional properties for Q1AVS9

Type Name Position InterPro Accession
domain AAA+ ATPase domain 200 - 346 IPR003593-1
domain AAA+ ATPase domain 600 - 758 IPR003593-2
domain ATPase, AAA-type, core 205 - 339 IPR003959-1
domain ATPase, AAA-type, core 599 - 764 IPR003959-2
domain Clp, repeat (R) domain 3 - 148 IPR004176
conserved_site ClpA/B, conserved site 1 296 - 308 IPR018368
domain Clp ATPase, C-terminal 771 - 860 IPR019489
conserved_site ClpA/B, conserved site 2 634 - 652 IPR028299
domain ClpA/ClpB, AAA lid domain 344 - 444 IPR041546

Functions

Description
EC Number 3.4.21.92 Serine endopeptidases
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

2 GO annotations of molecular function

Name Definition
ATP-dependent peptidase activity Catalysis of the hydrolysis of peptide bonds, driven by ATP hydrolysis.
serine-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).

1 GO annotations of biological process

Name Definition
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSYYDPQGVI PYVIEQSPRG ERAMDIYSRL LKDRIIFLGT PVDDQVANAI MAQLLHLESE
70 80 90 100 110 120
DPEQDINLYI NSPGGSVSAG LAIYDTMQFV KPDIVTTALG MAASMGAFLL AAGTKGKRFA
130 140 150 160 170 180
LPNTRILLHQ PAVGGLAGQA SDVEIHAREL IRTKRRLNEI LSEHTGQPYD KIERDTDRDF
190
IMGAEEAIEY GLIDDIVRHH