P0A9L3

PR
Gene name
fklB (ytfC, b4207, JW5746)
Protein name
FKBP-type 22 kDa peptidyl-prolyl cis-trans isomerase
Names
FKBP22, PPIase, Rotamase
Species
Escherichia coli (strain K12)
KEGG Pathway
eco:b4207
EC number
5.2.1.8: Cis-trans isomerases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

19-128 (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 P0A9L3

Entry ID Method Resolution Chain Position Source
AF-P0A9L3-F1 Predicted AlphaFoldDB

No variants for P0A9L3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P0A9L3

No associated diseases with P0A9L3

No regional properties for P0A9L3

Type Name Position InterPro Accession
No domain, repeats, and functional sites for P0A9L3

Functions

Description
EC Number 5.2.1.8 Cis-trans isomerases
Subcellular Localization
  • Cytoplasm
  • Periplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
periplasmic space The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria).

3 GO annotations of molecular function

Name Definition
FK506 binding Binding to a 23-membered macrolide lactone FK506.
identical protein binding Binding to an identical protein or proteins.
peptidyl-prolyl cis-trans isomerase activity Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0).

3 GO annotations of biological process

Name Definition
chaperone-mediated protein folding The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.
protein peptidyl-prolyl isomerization The modification of a protein by cis-trans isomerization of a proline residue.
protein refolding The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTTPTFDTIE AQASYGIGLQ VGQQLSESGL EGLLPEALVA GIADALEGKH PAVPVDVVHR
70 80 90 100 110 120
ALREIHERAD AVRRQRFQAM AAEGVKYLEE NAKKEGVNST ESGLQFRVIN QGEGAIPART
130 140 150 160 170 180
DRVRVHYTGK LIDGTVFDSS VARGEPAEFP VNGVIPGWIE ALTLMPVGSK WELTIPQELA
190 200
YGERGAGASI PPFSTLVFEV ELLEIL