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Protein

Trigger factor

Gene

tig

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).By similarity

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

GO - Molecular functioni

  • peptidyl-prolyl cis-trans isomerase activity Source: TIGR

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • protein folding Source: TIGR
  • protein transport Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase, Rotamase

Keywords - Biological processi

Cell cycle, Cell division

Enzyme and pathway databases

BioCyciVCHO:VC1923-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Trigger factor (EC:5.2.1.8)
Short name:
TF
Alternative name(s):
PPIase
Gene namesi
Name:tig
Ordered Locus Names:VC_1923
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
Proteomesi
  • UP000000584 Componenti: Chromosome 1

Subcellular locationi

  • Cytoplasm

  • Note: About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001794571 – 433Trigger factorAdd BLAST433

Proteomic databases

PRIDEiQ9KQS5.

Interactioni

Protein-protein interaction databases

STRINGi243277.VC1923.

Structurei

Secondary structure

1433
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 7Combined sources6
Beta strandi12 – 19Combined sources8
Helixi21 – 36Combined sources16
Helixi51 – 81Combined sources31
Beta strandi86 – 88Combined sources3
Beta strandi91 – 96Combined sources6
Beta strandi103 – 111Combined sources9
Beta strandi124 – 128Combined sources5
Helixi136 – 148Combined sources13
Beta strandi150 – 153Combined sources4
Beta strandi163 – 175Combined sources13
Beta strandi181 – 188Combined sources8
Helixi199 – 201Combined sources3
Turni202 – 204Combined sources3
Beta strandi213 – 216Combined sources4
Turni224 – 226Combined sources3
Beta strandi230 – 233Combined sources4
Beta strandi237 – 244Combined sources8
Helixi251 – 256Combined sources6
Turni258 – 261Combined sources4
Helixi262 – 287Combined sources26
Turni288 – 290Combined sources3
Beta strandi300 – 302Combined sources3
Helixi304 – 321Combined sources18
Helixi326 – 329Combined sources4
Helixi334 – 336Combined sources3
Helixi338 – 357Combined sources20
Helixi364 – 376Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1T11X-ray2.50A/B1-389[»]
ProteinModelPortaliQ9KQS5.
SMRiQ9KQS5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9KQS5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini161 – 246PPIase FKBP-typeAdd BLAST86

Domaini

Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.By similarity

Sequence similaritiesi

Belongs to the FKBP-type PPIase family. Tig subfamily.Curated
Contains 1 PPIase FKBP-type domain.Curated

Phylogenomic databases

eggNOGiENOG4105DEA. Bacteria.
COG0544. LUCA.
KOiK03545.
OMAiKAQNDDK.

Family and domain databases

Gene3Di1.10.3120.10. 1 hit.
3.30.70.1050. 1 hit.
HAMAPiMF_00303. Trigger_factor_Tig. 1 hit.
InterProiIPR001179. PPIase_FKBP_dom.
IPR005215. Trig_fac.
IPR008880. Trigger_fac_C.
IPR008881. Trigger_fac_ribosome-bd_bac.
IPR027304. Trigger_fact/SurA_dom.
[Graphical view]
PfamiPF00254. FKBP_C. 1 hit.
PF05698. Trigger_C. 1 hit.
PF05697. Trigger_N. 1 hit.
[Graphical view]
PIRSFiPIRSF003095. Trigger_factor. 1 hit.
SUPFAMiSSF102735. SSF102735. 1 hit.
SSF109998. SSF109998. 1 hit.
TIGRFAMsiTIGR00115. tig. 1 hit.
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9KQS5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQVTVETLEG LQRRLNITVP AANIEDAVAA ELRNIAKNRR FDGFRKGKVP
60 70 80 90 100
MKMVAKMYGK AVRQDVLGEV MQRHFIEAIV KEKINPAGAP TFAPVEIGEG
110 120 130 140 150
KDLVFTATFE VYPEVELKGL ENIAVEKPAA EVTDADVAEM LETLRKQQAT
160 170 180 190 200
WKEVDEAAEN GKRVSIDFVG SIDGVEFEGG KAENFPLEMG AGRMIPGFED
210 220 230 240 250
GIVGKTKGME FVIDVTFPED YHAENLKGKA AKFAIKVNKV EARELPELND
260 270 280 290 300
EFVARFGVAE GGVDALKAEV RKNMERELKQ AIKARIKEQA IEGLVKENEI
310 320 330 340 350
QVPSALIDQE INVLRQQAAQ RFGGNVEAAA QLPRELFEEQ AKRRVVVGLL
360 370 380 390 400
LGEVIRTHEL KADEEKVKAL ITEMATAYED PSEVVSYYEQ NQQLMNNMRN
410 420 430
VALEEQAVDA IIAKAKVTEK AISFSELMNP VAA
Length:433
Mass (Da):47,954
Last modified:October 1, 2000 - v1
Checksum:i23A889FA74C4510A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF95071.1.
PIRiH82139.
RefSeqiNP_231557.1. NC_002505.1.
WP_001198446.1. NC_002505.1.

Genome annotation databases

EnsemblBacteriaiAAF95071; AAF95071; VC_1923.
GeneIDi2613552.
KEGGivch:VC1923.
PATRICi20082890. VBIVibCho83274_1840.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF95071.1.
PIRiH82139.
RefSeqiNP_231557.1. NC_002505.1.
WP_001198446.1. NC_002505.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1T11X-ray2.50A/B1-389[»]
ProteinModelPortaliQ9KQS5.
SMRiQ9KQS5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243277.VC1923.

Proteomic databases

PRIDEiQ9KQS5.

Protocols and materials databases

DNASUi2613552.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF95071; AAF95071; VC_1923.
GeneIDi2613552.
KEGGivch:VC1923.
PATRICi20082890. VBIVibCho83274_1840.

Phylogenomic databases

eggNOGiENOG4105DEA. Bacteria.
COG0544. LUCA.
KOiK03545.
OMAiKAQNDDK.

Enzyme and pathway databases

BioCyciVCHO:VC1923-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9KQS5.

Family and domain databases

Gene3Di1.10.3120.10. 1 hit.
3.30.70.1050. 1 hit.
HAMAPiMF_00303. Trigger_factor_Tig. 1 hit.
InterProiIPR001179. PPIase_FKBP_dom.
IPR005215. Trig_fac.
IPR008880. Trigger_fac_C.
IPR008881. Trigger_fac_ribosome-bd_bac.
IPR027304. Trigger_fact/SurA_dom.
[Graphical view]
PfamiPF00254. FKBP_C. 1 hit.
PF05698. Trigger_C. 1 hit.
PF05697. Trigger_N. 1 hit.
[Graphical view]
PIRSFiPIRSF003095. Trigger_factor. 1 hit.
SUPFAMiSSF102735. SSF102735. 1 hit.
SSF109998. SSF109998. 1 hit.
TIGRFAMsiTIGR00115. tig. 1 hit.
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTIG_VIBCH
AccessioniPrimary (citable) accession number: Q9KQS5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: October 1, 2000
Last modified: November 2, 2016
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.