Q7N227

PR
Gene name
hscB
Protein name
Co-chaperone protein HscB
Names
Hsc20
Species
Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01)
KEGG Pathway
plu:plu3280
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

2-72 (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 Q7N227

Entry ID Method Resolution Chain Position Source
AF-Q7N227-F1 Predicted AlphaFoldDB

No variants for Q7N227

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q7N227

No associated diseases with Q7N227

2 regional properties for Q7N227

Type Name Position InterPro Accession
domain DnaJ domain 1 - 74 IPR001623
domain Co-chaperone HscB, C-terminal oligomerisation domain 88 - 163 IPR009073

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

2 GO annotations of molecular function

Name Definition
ATPase activator activity Binds to and increases the activity of an ATP hydrolysis activity.
chaperone binding Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.

3 GO annotations of biological process

Name Definition
[2Fe-2S] cluster assembly The incorporation of two iron atoms and two sulfur atoms into an iron-sulfur cluster.
protein complex oligomerization The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of component monomers; protein oligomers may be composed of different or identical monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.
protein folding The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MDYFTLFGLP ARYTVDREQL ASCYQELQRQ FHPDRFASQP EREKTLALQQ AVTINDGYQT
70 80 90 100 110 120
LKHPLKRAEY MLSLHGFDLA NEQHTMNDNA FLMEQLMLRE ELECIADKAN PEVALADFAA
130 140 150 160 170
RLNGMIKTRS QLMVQQLDEQ QWEQAADTVR KLRFLDKLQQ QVEQLEERLL DDF