UniProt Accession

 TIG_ECOLI; P0A850; P15299; P22257; P77603; Q2MBZ0 

Genbank Protein ID

 M34066; U00096; AP009048; U82664; X17642; J05534 

Genbank Nucleotide ID

 AAA62791.1; AAC73539.1; BAE76216.1; AAB40192.1; CAA35634.1; AAA23587.1 

Protein Name

 Trigger factor 

Protein Synonyms/Alias

 TF; PPIase 

Gene Name

 tig 

Gene Synonyms/Alias

 b0436; JW0426 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
37	SELVNVAKKVRIDGF	acetylation	[1]
38	ELVNVAKKVRIDGFR	acetylation	[1]
46	VRIDGFRKGKVPMNI	acetylation	[1]
48	IDGFRKGKVPMNIVA	acetylation	[1]
81	NFIDAIIKEKINPAG	acetylation	[1]
83	IDAIIKEKINPAGAP	acetylation	[1]
152	RKQQATWKEKDGAVE	acetylation	[1]
203	PGFEDGIKGHKAGEE	acetylation	[1]
227	EYHAENLKGKAAKFA	acetylation	[1]
232	NLKGKAAKFAINLKK	acetylation	[1]
238	AKFAINLKKVEEREL	acetylation	[1]
254	ELTAEFIKRFGVEDG	acetylation	[1, 2]
279	KNMERELKSAIRNRV	acetylation	[1]
296	QAIEGLVKANDIDVP	acetylation	[1]
327	QRFGGNEKQALELPR	acetylation	[1]
342	ELFEEQAKRRVVVGL	acetylation	[1]
361	VIRTNELKADEERVK	acetylation	[1]
382	ASAYEDPKEVIEFYS	acetylation	[1]
390	EVIEFYSKNKELMDN	acetylation	[1]
392	IEFYSKNKELMDNMR	acetylation	[1]
414	AVEAVLAKAKVTEKE	acetylation	[1, 3]
416	EAVLAKAKVTEKETT	acetylation	[1]
420	AKAKVTEKETTFNEL	acetylation	[1]

Reference

 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508]
 [3] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111] 

Functional Description

 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 (PubMed:12226666). Functions as a peptidyl-prolyl cis-trans isomerase in vitro, this activity is dispensible in vivo for chaperone activity. 

Sequence Annotation

 DOMAIN 161 246 PPIase FKBP-type.
 REGION 148 251 Dispensable for chaperone activity.  

Keyword

 3D-structure; Cell cycle; Cell division; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Isomerase; Reference proteome; Rotamase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 432 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:EcoCyc.
 GO:0044183; F:protein binding involved in protein folding; IDA:EcoCyc.
 GO:0043022; F:ribosome binding; IDA:EcoCyc.
 GO:0051083; P:'de novo' cotranslational protein folding; IDA:EcoCyc.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0006461; P:protein complex assembly; IPI:EcoCyc.
 GO:0015031; P:protein transport; IEA:HAMAP. 

Interpro

 IPR001179; PPIase_FKBP_dom.
 IPR005215; Trig_fac.
 IPR008880; Trigger_fac_C.
 IPR008881; Trigger_fac_ribosome-bd_bac.
 IPR027304; Trigger_fact/SurA_dom. 

Pfam

 PF00254; FKBP_C
 PF05698; Trigger_C
 PF05697; Trigger_N 

SMART

  

PROSITE

 PS50059; FKBP_PPIASE 

PRINTS