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Protein

Trigger factor

Gene

tig

Organism
Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195)
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

  1. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. protein folding Source: UniProtKB-HAMAP
  4. 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

BioCyciMGEN243273:GH2R-260-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:MG238
OrganismiMycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195)
Taxonomic identifieri243273 [NCBI]
Taxonomic lineageiBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma
ProteomesiUP000000807 Componenti: Chromosome

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

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Trigger factorPRO_0000179382Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243273.MG_238.

Structurei

Secondary structure

1
444
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi169 – 18113Combined sources
Beta strandi192 – 1987Combined sources
Helixi207 – 2126Combined sources
Beta strandi216 – 2227Combined sources
Beta strandi230 – 2334Combined sources
Helixi234 – 2363Combined sources
Beta strandi241 – 2466Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HXVNMR-A150-250[»]
ProteinModelPortaliP47480.
SMRiP47480. Positions 166-250.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP47480.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini170 – 25586PPIase FKBP-typeAdd
BLAST

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

eggNOGiCOG0544.
KOiK03545.
OMAiWAINIAF.
OrthoDBiEOG63VBX3.

Family and domain databases

Gene3Di1.10.3120.10. 1 hit.
3.30.70.1050. 1 hit.
HAMAPiMF_00303. Trigger_factor_Tig.
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.

P47480-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLYKVLNSK TTDKSLCLEV EIDPNYWQAT QKKLVGEMAK SIKIKGFRPG
60 70 80 90 100
KIPPNLASQS INKAELMQKS AQNVMNSIYE SVQQEEIVAS NDNVIDDYPT
110 120 130 140 150
IDFKTITEQN CVLLFYFDLI PNFQLPDYKK IKDLTPLTKL TEAEFNNEIE
160 170 180 190 200
KLAKTKSTMV DVSDKKLANG DIAIIDFTGI VDNKKLASAS AQNYELTIGS
210 220 230 240 250
NSFIKGFETG LIAMKVNQKK TLALTFPSDY HVKELQSKPV TFEVVLKAIK
260 270 280 290 300
KLEFTPMDET NFKSFLPEQF QSFTSLKAFK SYFHKLMENK KQETILQENN
310 320 330 340 350
QKIRQFLLTN TKLPFLPEAL IKLEANRLLK LQQSQAEQYK IPFEKLLSAS
360 370 380 390 400
NITLTELQDR NIKEAKENVT FALVMKKIAD IEKIKVDNNK IKAEIENVIA
410 420 430 440
VEYPFASDEM KKQLFFNMEQ QKEFVESIII NRLTTTKIVS YSTH
Length:444
Mass (Da):50,931
Last modified:February 1, 1996 - v1
Checksum:i99704A2EA4E23F47
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L43967 Genomic DNA. Translation: AAC71459.1.
U01772 Genomic DNA. Translation: AAD10591.1.
PIRiC64226.
RefSeqiNP_072904.1. NC_000908.2.

Genome annotation databases

EnsemblBacteriaiAAC71459; AAC71459; MG_238.
KEGGimge:MG_238.
PATRICi20009958. VBIMycGen98045_0275.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L43967 Genomic DNA. Translation: AAC71459.1.
U01772 Genomic DNA. Translation: AAD10591.1.
PIRiC64226.
RefSeqiNP_072904.1. NC_000908.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HXVNMR-A150-250[»]
ProteinModelPortaliP47480.
SMRiP47480. Positions 166-250.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243273.MG_238.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC71459; AAC71459; MG_238.
KEGGimge:MG_238.
PATRICi20009958. VBIMycGen98045_0275.

Phylogenomic databases

eggNOGiCOG0544.
KOiK03545.
OMAiWAINIAF.
OrthoDBiEOG63VBX3.

Enzyme and pathway databases

BioCyciMGEN243273:GH2R-260-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP47480.

Family and domain databases

Gene3Di1.10.3120.10. 1 hit.
3.30.70.1050. 1 hit.
HAMAPiMF_00303. Trigger_factor_Tig.
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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 33530 / G-37 / NCTC 10195.
  2. "A survey of the Mycoplasma genitalium genome by using random sequencing."
    Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III
    J. Bacteriol. 175:7918-7930(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 141-216.
    Strain: ATCC 33530 / G-37 / NCTC 10195.
  3. "NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain of the trigger factor from Mycoplasma genitalium compared to FK506-binding protein."
    Vogtherr M., Jacobs D.M., Parac T.N., Maurer M., Pahl A., Saxena K., Rueterjans H., Griesinger C., Fiebig K.M.
    J. Mol. Biol. 318:1097-1115(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 166-250.

Entry informationi

Entry nameiTIG_MYCGE
AccessioniPrimary (citable) accession number: P47480
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 1, 2015
This is version 104 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

Documents

  1. Mycoplasma genitalium
    Mycoplasma genitalium (strain G-37): entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.