P0A850 (TIG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Trigger factor
Short name=TF
EC=5.2.1.8

Alternative name(s):
PPIase

Gene names

Name:	tig
Ordered Locus Names:	b0436, JW0426

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	432 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in protein export. Acts as a chaperone by maintaining the newly synthesized secretory and non-secretory proteins in an open conformation. Binds to nascent polypeptide chains via ribosomal protein L23 (Ref.14). Functions as a peptidyl-prolyl cis-trans isomerase in vitro, this activity is dispensible in vivo for chaperone activity. Ref.8 Ref.11 Ref.16
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0). HAMAP-Rule MF_00303
Subunit structure	Homodimer and monomer. In vivo most of the ribosomes are in complex with monomeric TF (Ref.13); binding as a dimer has also been suggested (Ref.17). Uncomplexed TF is in a monomer-dimer equilibrium with approximately two thirds of TF existing in a dimeric state. TF and SRP can simultaneously bind to ribosomes; TF binding is abolished when SRP is bound to FtsY in the presence of a non-hydrolyzable GTP analog (Ref.18). Contacts ribosomal proteins L23 and L29 (Ref.14). Ref.13
Subcellular location	Cytoplasm. Note: About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm. Ref.8
Domain	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. Ref.16
Disruption phenotype	Non-essential; synthetic lethality is seen in a triple tig-dnaK-dnaJ disruption, although this depends on temperature (triple disruptions grow slowly at 20 and 34 degrees Celsius but not at all at 43 degrees) and strain background. Ref.16
Sequence similarities	Belongs to the FKBP-type PPIase family. Tig subfamily. Contains 1 PPIase FKBP-type domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Cytoplasm
Molecular function	Chaperone Isomerase Rotamase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' cotranslational protein folding Inferred from direct assay Ref.8. Source: EcoCyc cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW protein complex assembly Inferred from physical interaction PubMed 19737520. Source: EcoCyc protein transport Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB membrane Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	peptidyl-prolyl cis-trans isomerase activity Inferred from direct assay Ref.8. Source: EcoCyc protein binding involved in protein folding Inferred from direct assay Ref.8. Source: EcoCyc ribosome binding Inferred from direct assay Ref.8. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-544862,EBI-544862
ompA	P0A910	3	EBI-544862,EBI-371347
rpsG	P02359	3	EBI-544862,EBI-543074

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 432

432

Trigger factor HAMAP-Rule MF_00303

PRO_0000179347

Regions

Domain

161 – 246

86

PPIase FKBP-type

Region

148 – 251

104

Dispensable for chaperone activity HAMAP-Rule MF_00303

Experimental info

Mutagenesis

44 – 46

3

FRK → AAA: Decreases association with ribosomes. Ref.14

Sequence conflict

118

1

Q → E in AAA62791. Ref.1

Sequence conflict

279 – 287

9

KSAIRNRVK → RAPSVTALS in AAA62791. Ref.1

Secondary structure

1

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432

Helix Strand Turn

Details...

Beta strand

2 – 7

6

Beta strand

12 – 19

8

Helix

21 – 36

16

Helix

42 – 44

3

Beta strand

46 – 48

3

Helix

51 – 81

31

Beta strand

87 – 94

8

Beta strand

99 – 101

3

Beta strand

103 – 110

8

Turn

120 – 122

3

Beta strand

127 – 129

3

Helix

134 – 147

14

Beta strand

155 – 157

3

Beta strand

163 – 166

4

Beta strand

168 – 174

7

Beta strand

183 – 188

6

Helix

198 – 201

4

Beta strand

202 – 204

3

Beta strand

210 – 216

7

Turn

224 – 226

3

Beta strand

230 – 236

7

Helix

250 – 253

4

Turn

254 – 257

4

Helix

263 – 297

35

Helix

304 – 319

16

Turn

320 – 323

4

Helix

334 – 336

3

Helix

338 – 357

20

Helix

364 – 375

12

Helix

381 – 390

10

Helix

392 – 412

21

Beta strand

419 – 421

3

Helix

424 – 427

4

Sequences

	Sequence		Length	Mass (Da)
	P0A850 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: 42C3E3C335074164	FASTA	432	48,193
	10 20 30 40 50 60 MQVSVETTQG LGRRVTITIA ADSIETAVKS ELVNVAKKVR IDGFRKGKVP MNIVAQRYGA 70 80 90 100 110 120 SVRQDVLGDL MSRNFIDAII KEKINPAGAP TYVPGEYKLG EDFTYSVEFE VYPEVELQGL 130 140 150 160 170 180 EAIEVEKPIV EVTDADVDGM LDTLRKQQAT WKEKDGAVEA EDRVTIDFTG SVDGEEFEGG 190 200 210 220 230 240 KASDFVLAMG QGRMIPGFED GIKGHKAGEE FTIDVTFPEE YHAENLKGKA AKFAINLKKV 250 260 270 280 290 300 EERELPELTA EFIKRFGVED GSVEGLRAEV RKNMERELKS AIRNRVKSQA IEGLVKANDI 310 320 330 340 350 360 DVPAALIDSE IDVLRRQAAQ RFGGNEKQAL ELPRELFEEQ AKRRVVVGLL LGEVIRTNEL 370 380 390 400 410 420 KADEERVKGL IEEMASAYED PKEVIEFYSK NKELMDNMRN VALEEQAVEA VLAKAKVTEK 430 ETTFNELMNQ QA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Trigger factor depletion or overproduction causes defective cell division but does not block protein export." Guthrie B., Wickner W. J. Bacteriol. 172:5555-5562(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: K12.
[2]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Induction of a growth-phase-dependent promoter triggers transcription of bolA, an Escherichia coli morphogene." Aldea M., Garrido T., Hernandez-Chico C., Vicente M., Kushner S.R. EMBO J. 8:3923-3931(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-145.
[6]	"ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle." Crooke E., Guthrie B., Lecker S., Lill R., Wickner W. Cell 54:1003-1011(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-13.
[7]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-21 AND 38-58. Strain: K12 / EMG2.
[8]	"Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains." Hesterkamp T., Hauser S., Lutcke H., Bukau B. Proc. Natl. Acad. Sci. U.S.A. 93:4437-4441(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-7, FUNCTION AS A PPIASE, SUBCELLULAR LOCATION, RIBOSOME-BINDING.
[9]	"An 11.8 kDa proteolytic fragment of the E. coli trigger factor represents the domain carrying the peptidyl-prolyl cis/trans isomerase activity." Stoller G., Tradler T., Ruecknagel K.P., Rahfeld J.-U., Fischer G. FEBS Lett. 384:117-122(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 145-174.
[10]	"Sequence and structure of Clp P, the proteolytic component of the ATP-dependent Clp protease of Escherichia coli." Maurizi M.R., Clark W.P., Katayama Y., Rudikoff S., Pumphrey J., Bowers B., Gottesman S. J. Biol. Chem. 265:12536-12545(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 390-432.
[11]	"Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides." Valent Q.A., Kendall D.A., High S., Kusters R., Oudega B., Luirink J. EMBO J. 14:5494-5505(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[13]	"Three-state equilibrium of Escherichia coli trigger factor." Patzelt H., Kramer G., Rauch T., Schonfeld H.J., Bukau B., Deuerling E. Biol. Chem. 383:1611-1619(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT.
[14]	"L23 protein functions as a chaperone docking site on the ribosome." Kramer G., Rauch T., Rist W., Vorderwuelbecke S., Patzelt H., Schulze-Specking A., Ban N., Deuerling E., Bukau B. Nature 419:171-174(2002) [PubMed] [Europe PMC] [Abstract] Cited for: BINDING TO RIBOSOMAL PROTEINS L23 AND L29, MUTAGENESIS OF 44-PHE--LYS-46. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[15]	"Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome." Ullers R.S., Houben E.N.G., Raine A., ten Hagen-Jongman C.M., Ehrenberg M., Brunner J., Oudega B., Harms N., Luirink J. J. Cell Biol. 161:679-684(2003) [PubMed] [Europe PMC] [Abstract] Cited for: CROSS-LINKS TO NASCENT PROTEIN CHAINS. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[16]	"In vivo analysis of the overlapping functions of DnaK and trigger factor." Genevaux P., Keppel F., Schwager F., Langendijk-Genevaux P.S., Hartl F.U., Georgopoulos C. EMBO Rep. 5:195-200(2004) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN, DISPENSABILITY OF PPIASE FOR CHAPERONE FUNCTION, DISRUPTION PHENOTYPE. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[17]	"Localization of the trigger factor binding site on the ribosomal 50S subunit." Blaha G., Wilson D.N., Stoller G., Fischer G., Willumeit R., Nierhaus K.H. J. Mol. Biol. 326:887-897(2003) [PubMed] [Europe PMC] [Abstract] Cited for: MAY BIND TO THE RIBOSOME AS A DIMER. Strain: MRE-600.
[18]	"Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor." Buskiewicz I., Deuerling E., Gu S.-Q., Joeckel J., Rodnina M.V., Bukau B., Wintermeyer W. Proc. Natl. Acad. Sci. U.S.A. 101:7902-7906(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SIMULTANEOUS BINDING OF TRIGGER FACTOR AND SRP TO THE RIBOSOME. Strain: MRE-600.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M34066 Genomic DNA. Translation: AAA62791.1.
U00096 Genomic DNA. Translation: AAC73539.1.
AP009048 Genomic DNA. Translation: BAE76216.1.
U82664 Genomic DNA. Translation: AAB40192.1.
X17642 Genomic DNA. Translation: CAA35634.1.
J05534 Genomic DNA. Translation: AAA23587.1.

PIR

D64773.

RefSeq

NP_414970.1. NC_000913.2.
YP_488728.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1L1P	NMR	-	A	148-249	[»]
1OMS	X-ray	2.30	A/B/C	1-118	[»]
1P9Y	X-ray	2.15	A/B	1-118	[»]
1W26	X-ray	2.70	A/B	1-432	[»]
1W2B	X-ray	3.50	5	1-144	[»]
2VRH	electron microscopy	19.00	A	1-432	[»]

ProteinModelPortal

P0A850.

SMR

P0A850. Positions 1-432.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36226N.

IntAct

P0A850. 125 interactions.

MINT

MINT-1225982.

STRING

511145.b0436.

2D gel databases

SWISS-2DPAGE

P0A850.

Proteomic databases

PaxDb

P0A850.

PRIDE

P0A850.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73539; AAC73539; b0436.
BAE76216; BAE76216; BAE76216.

GeneID

12930847.
945081.

KEGG

ecj:Y75_p0424.
eco:b0436.

PATRIC

32116025. VBIEscCol129921_0454.

Organism-specific databases

EchoBASE

EB0996.

EcoGene

EG11003. tig.

Phylogenomic databases

eggNOG

COG0544.

HOGENOM

HOG000218239.

KO

K03545.

OMA

FPADYHG.

ProtClustDB

PRK01490.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11003-MONOMER.
ECOL316407:JW0426-MONOMER.
MetaCyc:EG11003-MONOMER.

Gene expression databases

Genevestigator

P0A850.

Family and domain databases

Gene3D

1.10.3120.10. 1 hit.
3.30.70.1050. 1 hit.

HAMAP

MF_00303. Trigger_factor_Tig.

InterPro

IPR001179. PPIase_FKBP_dom.
IPR005215. Trig_fac.
IPR008880. Trigger_fac_C.
IPR008881. Trigger_fac_ribosome-bd_bac.
IPR027304. Trigger_fact/SurA_dom.
[Graphical view]

Pfam

PF00254. FKBP_C. 1 hit.
PF05698. Trigger_C. 1 hit.
PF05697. Trigger_N. 1 hit.
[Graphical view]

PIRSF

PIRSF003095. Trigger_factor. 1 hit.

SUPFAM

SSF109998. Trigger_fac_C_bac. 1 hit.
SSF102735. Trigger_fac_ribosome-bd_bac. 1 hit.

TIGRFAMs

TIGR00115. tig. 1 hit.

PROSITE

PS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A850.

Entry information

Entry name

TIG_ECOLI

Accession

Primary (citable) accession number: P0A850
Secondary accession number(s): P15299 , P22257, P77603, Q2MBZ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	May 1, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program