RegulonDB RegulonDB 10.7: Gene Form
   

tig gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

tig clpP bolA terminator anti-terminator TSS_580 TSS_580 clpXp clpXp TSS_578 TSS_578 TSS_577 (cluster) TSS_577 (cluster) TSS_576 TSS_576 clpPp2 clpPp2 TSS_575 TSS_575 clpPp3 clpPp3 TSS_573 TSS_573 TSS_572 TSS_572 clpPp1 clpPp1 TSS_570 TSS_570 TSS_569 (cluster) TSS_569 (cluster) TSS_568 TSS_568 TSS_567 TSS_567 TSS_566 TSS_566 tigp3 tigp3 TSS_565 (cluster) TSS_565 (cluster) TSS_564 TSS_564 TSS_563 TSS_563 tigp tigp tigp1 tigp1 TSS_561 TSS_561

Gene      
Name: tig    Texpresso search in the literature
Synonym(s): ECK0430, EG11003, b0436
Genome position(nucleotides): 455133 --> 456431 Genome Browser
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
51.19
External database links:  
ASAP:
ABE-0001511
CGSC:
35681
ECHOBASE:
EB0996
OU-MICROARRAY:
b0436
PORTECO:
tig
REGULONDB:
b0436
STRING:
511145.b0436
M3D: tig
COLOMBOS: tig
PortEco: b0436


Product      
Name: trigger factor
Synonym(s): Tig, chaperone protein Tig
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 48.193
Isoelectric point: 4.52
Motif(s):
 
Type Positions Sequence
150 -> 246 TWKEKDGAVEAEDRVTIDFTGSVDGEEFEGGKASDFVLAMGQGRMIPGFEDGIKGHKAGEEFTIDVTFPEEYHAENLKGKAAKFAINLKKVEERELP
118 -> 118 Q
158 -> 236 VEAEDRVTIDFTGSVDGEEFEGGKASDFVLAMGQGRMIPGFEDGIKGHKAGEEFTIDVTFPEEYHAENLKGKAAKFAIN
374 -> 387 MASAYEDPKEVIEF
44 -> 46 FRK

 

Classification:
Multifun Terms (GenProtEC)  
  2 - information transfer --> 2.3 - protein related --> 2.3.4 - chaperoning, repair (refolding)
  5 - cell processes --> 5.1 - cell division
Gene Ontology Terms (GO)  
cellular_component GO:0005737 - cytoplasm
GO:0005829 - cytosol
molecular_function GO:0005515 - protein binding
GO:0016853 - isomerase activity
GO:0043022 - ribosome binding
GO:0003755 - peptidyl-prolyl cis-trans isomerase activity
GO:0042802 - identical protein binding
GO:0044183 - protein folding chaperone
biological_process GO:0051301 - cell division
GO:0006457 - protein folding
GO:0007049 - cell cycle
GO:0009408 - response to heat
GO:0015031 - protein transport
GO:0065003 - protein-containing complex assembly
GO:0051083 - 'de novo' cotranslational protein folding
GO:0061077 - chaperone-mediated protein folding
GO:0043335 - protein unfolding
GO:0000413 - protein peptidyl-prolyl isomerization
Note(s): Note(s): ...[more].
Reference(s): [1] Crooke E., et al., 1988
[2] Eisner G., et al., 2006
[3] Kramer G., et al., 2004
[4] Lill R., et al., 1988
[5] Liu CP., et al., 2010
[6] Raine A., et al., 2004
[7] Schaffitzel E., et al., 2001
[8] Stoller G., et al., 1996
[9] Teter SA., et al., 1999
[10] Ullers RS., et al., 2006
[11] Ullers RS., et al., 2003
[12] Valent QA., et al., 1997
[13] Wasinger VC., et al., 1998
External database links:  
DIP:
DIP-36226N
ECOCYC:
EG11003-MONOMER
ECOLIWIKI:
b0436
INTERPRO:
IPR008881
INTERPRO:
IPR008880
INTERPRO:
IPR005215
INTERPRO:
IPR027304
INTERPRO:
IPR036611
INTERPRO:
IPR037041
INTERPRO:
IPR001179
MINT:
MINT-1225982
MODBASE:
P0A850
PANTHER:
PTHR30560
PDB:
6D6S
PDB:
5ZR0
PDB:
5OWJ
PDB:
5OWI
PDB:
4URD
PDB:
2VRH
PDB:
2MLZ
PDB:
2MLY
PDB:
2MLX
PDB:
1W2B
PDB:
1W26
PDB:
1P9Y
PDB:
1OMS
PDB:
1L1P
PFAM:
PF00254
PFAM:
PF05698
PFAM:
PF05697
PRIDE:
P0A850
PRODB:
PRO_000024070
PROSITE:
PS50059
PROTEINMODELPORTAL:
P0A850
REFSEQ:
NP_414970
SMR:
P0A850
UNIPROT:
P0A850


Operon      
Name: tig         
Operon arrangement:
Transcription unit        Promoter
 
 
tig


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter TSS_561 454664 forward nd [RS-EPT-CBR] [14]
  promoter tigp 454994 forward nd [AIPP], [RS-EPT-CBR] [14], [15]
  promoter TSS_563 454999 forward nd [RS-EPT-CBR] [14]
  promoter TSS_564 455004 forward nd [RS-EPT-CBR] [14]
  promoter TSS_565 (cluster) 455007 forward For this promoter, there
Read more >
[RS-EPT-CBR] [14]
  promoter TSS_566 455378 forward nd [RS-EPT-CBR] [14]
  promoter TSS_567 455382 forward nd [RS-EPT-CBR] [14]
  promoter TSS_568 455792 forward nd [RS-EPT-CBR] [14]
  promoter TSS_569 (cluster) 456551 forward For this promoter, there
Read more >
[RS-EPT-CBR] [14]
  promoter TSS_570 456560 forward nd [RS-EPT-CBR] [14]
  promoter TSS_572 456594 forward nd [RS-EPT-CBR] [14]
  promoter TSS_573 456597 forward nd [RS-EPT-CBR] [14]
  promoter TSS_575 456643 forward nd [RS-EPT-CBR] [14]
  promoter TSS_576 457052 forward nd [RS-EPT-CBR] [14]
  promoter TSS_577 (cluster) 457151 forward For this promoter, there
Read more >
[RS-EPT-CBR] [14]
  promoter TSS_578 457171 forward nd [RS-EPT-CBR] [14]
  promoter TSS_580 457296 forward nd [RS-EPT-CBR] [14]


Evidence    

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates

 [AIPP] Automated inference of promoter position



Reference(s)    

 [1] Crooke E., Brundage L., Rice M., Wickner W., 1988, ProOmpA spontaneously folds in a membrane assembly competent state which trigger factor stabilizes., EMBO J 7(6):1831-5

 [2] Eisner G., Moser M., Schafer U., Beck K., Muller M., 2006, Alternate recruitment of signal recognition particle and trigger factor to the signal sequence of a growing nascent polypeptide., J Biol Chem 281(11):7172-9

 [3] Kramer G., Rutkowska A., Wegrzyn RD., Patzelt H., Kurz TA., Merz F., Rauch T., Vorderwulbecke S., Deuerling E., Bukau B., 2004, Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains., J Bacteriol 186(12):3777-84

 [4] Lill R., Crooke E., Guthrie B., Wickner W., 1988, The "trigger factor cycle" includes ribosomes, presecretory proteins, and the plasma membrane., Cell 54(7):1013-8

 [5] Liu CP., Zhou QM., Fan DJ., Zhou JM., 2010, PPIase domain of trigger factor acts as auxiliary chaperone site to assist the folding of protein substrates bound to the crevice of trigger factor., Int J Biochem Cell Biol 42(6):890-901

 [6] Raine A., Ivanova N., Wikberg JE., Ehrenberg M., 2004, Simultaneous binding of trigger factor and signal recognition particle to the E. coli ribosome., Biochimie 86(7):495-500

 [7] Schaffitzel E., Rudiger S., Bukau B., Deuerling E., 2001, Functional dissection of trigger factor and DnaK: interactions with nascent polypeptides and thermally denatured proteins., Biol Chem 382(8):1235-43

 [8] Stoller G., Tradler T., Rucknagel KP., Rahfeld J-U., Fischer G., 1996, An 11.8 kDa proteolytic fragment of the E. coli trigger factor represents the domain carrying the peptidyl-prolyl cis/trans isomerase activity., FEBS Lett 384(2):117-22

 [9] Teter SA., Houry WA., Ang D., Tradler T., Rockabrand D., Fischer G., Blum P., Georgopoulos C., Hartl FU., 1999, Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains., Cell 97(6):755-65

 [10] Ullers RS., Houben EN., Brunner J., Oudega B., Harms N., Luirink J., 2006, Sequence-specific interactions of nascent Escherichia coli polypeptides with trigger factor and signal recognition particle., J Biol Chem 281(20):13999-4005

 [11] Ullers RS., Houben EN., Raine A., ten Hagen-Jongman CM., Ehrenberg M., Brunner J., Oudega B., Harms N., Luirink J., 2003, Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome., J Cell Biol 161(4):679-84

 [12] Valent QA., de Gier JW., von Heijne G., Kendall DA., ten Hagen-Jongman CM., Oudega B., Luirink J., 1997, Nascent membrane and presecretory proteins synthesized in Escherichia coli associate with signal recognition particle and trigger factor., Mol Microbiol 25(1):53-64

 [13] Wasinger VC., Humphery-Smith I., 1998, Small genes/gene-products in Escherichia coli K-12., FEMS Microbiol Lett 169(2):375-82

 [14] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.

 [15] Aldea M., Garrido T., Hernandez-Chico C., Vicente M., Kushner SR., 1989, Induction of a growth-phase-dependent promoter triggers transcription of bolA, an Escherichia coli morphogene., EMBO J 8(12):3923-31


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