Q83DJ3

PR
Gene name
tig
Protein name
Trigger factor
Names
TF, PPIase
Species
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
KEGG Pathway
cbu:CBU_0737
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)

295-430 (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 Q83DJ3

Entry ID Method Resolution Chain Position Source
AF-Q83DJ3-F1 Predicted AlphaFoldDB

No variants for Q83DJ3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q83DJ3

No associated diseases with Q83DJ3

3 regional properties for Q83DJ3

Type Name Position InterPro Accession
domain FKBP-type peptidyl-prolyl cis-trans isomerase domain 160 - 255 IPR001179
domain Trigger factor, C-terminal 267 - 420 IPR008880
domain Trigger factor, ribosome-binding, bacterial 8 - 147 IPR008881

Functions

Description
EC Number 5.2.1.8 Cis-trans isomerases
Subcellular Localization
  • Cytoplasm
  • About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the 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.

3 GO annotations of molecular function

Name Definition
peptidyl-prolyl cis-trans isomerase activity Catalysis of the reaction: peptidyl-proline (omega=180) = peptidyl-proline (omega=0).
protein folding chaperone Binding to a protein or a protein-containing complex to assist the protein folding process.
ribosome binding Binding to a ribosome.

6 GO annotations of biological process

Name Definition
'de novo' cotranslational protein folding The process of assisting in the correct noncovalent assembly of the ribosome-bound nascent chains of a multidomain protein whilst other parts of the protein are still being translated.
cell cycle The progression of biochemical and morphological phases and events that occur in a cell during successive cell replication or nuclear replication events. Canonically, the cell cycle comprises the replication and segregation of genetic material followed by the division of the cell, but in endocycles or syncytial cells nuclear replication or nuclear division may not be followed by cell division.
cell division The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells.
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 transport The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
protein unfolding The process of assisting in the disassembly of non-covalent linkages in a protein or protein aggregate, often where the proteins are in a non-functional or denatured state.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MRGNFMSSIE KLGGLKQRLT ITVPAEEVDK AYKSRLLKVA RTAKIPKFRP GKASPAVVEK
70 80 90 100 110 120
LYGKAILQEV GSELIQSSLR EAVEEHQLRV AGAPDIKMDK ILRGEPFKYV VNFEVYPEIT
130 140 150 160 170 180
LESLAGETIE RTQVEITEED LDKMLEALRK QYAEWKEMDR PAKADDRVII DFEGTLDGKP
190 200 210 220 230 240
FERGSAKDFQ LELGSKRMIA GFEEGIEGMK PGESKALDIT FPADYPSEDL AGKAAVFNIT
250 260 270 280 290 300
LQKVMAPELP VLDEQFAERL GIKEGGLEAL RQKVRTNMEK EVHHHMENKL KMAVLDKLIE
310 320 330 340 350 360
RNPIEVPESL IEAEIDHLQQ MTRQQVAMQT HKPDEAKKME LPRDPYREQA TKRVKLGLLL
370 380 390 400 410 420
AEVVKQHKIK ADPEQLRARV EEVAASYQDP EKVISWYYTN KQMLSEIESV VLEDQAVAQL
430 440
MSELEVKDQA IPYEEAVKQI QQ