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P0A850

- TIG_ECOLI

UniProt

P0A850 - TIG_ECOLI

Protein

Trigger factor

Gene

tig

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (07 Jun 2005)
      Previous versions | rss
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    Functioni

    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.3 Publications

    Catalytic activityi

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

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. peptidyl-prolyl cis-trans isomerase activity Source: EcoCyc
    3. protein binding Source: IntAct
    4. protein binding involved in protein folding Source: EcoCyc
    5. ribosome binding Source: EcoCyc

    GO - Biological processi

    1. 'de novo' cotranslational protein folding Source: EcoCyc
    2. cell cycle Source: UniProtKB-KW
    3. cell division Source: UniProtKB-KW
    4. protein peptidyl-prolyl isomerization Source: GOC
    5. protein transport Source: UniProtKB-HAMAP
    6. response to heat Source: EcoCyc

    Keywords - Molecular functioni

    Chaperone, Isomerase, Rotamase

    Keywords - Biological processi

    Cell cycle, Cell division

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11003-MONOMER.
    ECOL316407:JW0426-MONOMER.
    MetaCyc:EG11003-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:b0436, JW0426
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11003. tig.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm.

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    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.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi44 – 463FRK → AAA: Decreases association with ribosomes. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 432432Trigger factorPRO_0000179347Add
    BLAST

    Proteomic databases

    PaxDbiP0A850.
    PRIDEiP0A850.

    2D gel databases

    SWISS-2DPAGEP0A850.

    Expressioni

    Gene expression databases

    GenevestigatoriP0A850.

    Interactioni

    Subunit structurei

    Homodimer and monomer. In vivo most of the ribosomes are in complex with monomeric TF (PubMed:12452438); binding as a dimer has also been suggested (PubMed:12581648). 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 (PubMed:15148364). Contacts ribosomal proteins L23 and L29 (PubMed:12226666).4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-544862,EBI-544862
    ompAP0A9103EBI-544862,EBI-371347
    rpsGP023593EBI-544862,EBI-543074

    Protein-protein interaction databases

    DIPiDIP-36226N.
    IntActiP0A850. 125 interactions.
    MINTiMINT-1225982.
    STRINGi511145.b0436.

    Structurei

    Secondary structure

    1
    432
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 76
    Beta strandi12 – 198
    Helixi21 – 3616
    Helixi42 – 443
    Beta strandi46 – 483
    Helixi51 – 8131
    Beta strandi87 – 948
    Beta strandi99 – 1013
    Beta strandi103 – 1108
    Turni120 – 1223
    Beta strandi127 – 1293
    Helixi134 – 14714
    Beta strandi155 – 1573
    Beta strandi163 – 1664
    Beta strandi168 – 1747
    Beta strandi183 – 1886
    Helixi198 – 2014
    Beta strandi202 – 2043
    Beta strandi210 – 2167
    Turni224 – 2263
    Beta strandi230 – 2367
    Helixi250 – 2534
    Turni254 – 2574
    Helixi263 – 29735
    Helixi304 – 31916
    Turni320 – 3234
    Helixi334 – 3363
    Helixi338 – 35720
    Helixi364 – 37512
    Helixi381 – 39010
    Helixi392 – 41221
    Beta strandi419 – 4213
    Helixi424 – 4274

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1L1PNMR-A148-249[»]
    1OMSX-ray2.30A/B/C1-118[»]
    1P9YX-ray2.15A/B1-118[»]
    1W26X-ray2.70A/B1-432[»]
    1W2BX-ray3.5051-144[»]
    2VRHelectron microscopy19.00A1-432[»]
    ProteinModelPortaliP0A850.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0A850.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini161 – 24686PPIase FKBP-typeAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni148 – 251104Dispensable for chaperone activityAdd
    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.1 Publication

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0544.
    HOGENOMiHOG000218239.
    KOiK03545.
    OMAiMQVSVEN.
    OrthoDBiEOG63VBX3.
    PhylomeDBiP0A850.

    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.

    P0A850-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQVSVETTQG LGRRVTITIA ADSIETAVKS ELVNVAKKVR IDGFRKGKVP    50
    MNIVAQRYGA SVRQDVLGDL MSRNFIDAII KEKINPAGAP TYVPGEYKLG 100
    EDFTYSVEFE VYPEVELQGL EAIEVEKPIV EVTDADVDGM LDTLRKQQAT 150
    WKEKDGAVEA EDRVTIDFTG SVDGEEFEGG KASDFVLAMG QGRMIPGFED 200
    GIKGHKAGEE FTIDVTFPEE YHAENLKGKA AKFAINLKKV EERELPELTA 250
    EFIKRFGVED GSVEGLRAEV RKNMERELKS AIRNRVKSQA IEGLVKANDI 300
    DVPAALIDSE IDVLRRQAAQ RFGGNEKQAL ELPRELFEEQ AKRRVVVGLL 350
    LGEVIRTNEL KADEERVKGL IEEMASAYED PKEVIEFYSK NKELMDNMRN 400
    VALEEQAVEA VLAKAKVTEK ETTFNELMNQ QA 432
    Length:432
    Mass (Da):48,193
    Last modified:June 7, 2005 - v1
    Checksum:i42C3E3C335074164
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti118 – 1181Q → E in AAA62791. (PubMed:2211496)Curated
    Sequence conflicti279 – 2879KSAIRNRVK → RAPSVTALS in AAA62791. (PubMed:2211496)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiD64773.
    RefSeqiNP_414970.1. NC_000913.3.
    YP_488728.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73539; AAC73539; b0436.
    BAE76216; BAE76216; BAE76216.
    GeneIDi12930847.
    945081.
    KEGGiecj:Y75_p0424.
    eco:b0436.
    PATRICi32116025. VBIEscCol129921_0454.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi D64773.
    RefSeqi NP_414970.1. NC_000913.3.
    YP_488728.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P0A850.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-36226N.
    IntActi P0A850. 125 interactions.
    MINTi MINT-1225982.
    STRINGi 511145.b0436.

    2D gel databases

    SWISS-2DPAGE P0A850.

    Proteomic databases

    PaxDbi P0A850.
    PRIDEi P0A850.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73539 ; AAC73539 ; b0436 .
    BAE76216 ; BAE76216 ; BAE76216 .
    GeneIDi 12930847.
    945081.
    KEGGi ecj:Y75_p0424.
    eco:b0436.
    PATRICi 32116025. VBIEscCol129921_0454.

    Organism-specific databases

    EchoBASEi EB0996.
    EcoGenei EG11003. tig.

    Phylogenomic databases

    eggNOGi COG0544.
    HOGENOMi HOG000218239.
    KOi K03545.
    OMAi MQVSVEN.
    OrthoDBi EOG63VBX3.
    PhylomeDBi P0A850.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTracei P0A850.
    PROi P0A850.

    Gene expression databases

    Genevestigatori P0A850.

    Family and domain databases

    Gene3Di 1.10.3120.10. 1 hit.
    3.30.70.1050. 1 hit.
    HAMAPi MF_00303. Trigger_factor_Tig.
    InterProi IPR001179. PPIase_FKBP_dom.
    IPR005215. Trig_fac.
    IPR008880. Trigger_fac_C.
    IPR008881. Trigger_fac_ribosome-bd_bac.
    IPR027304. Trigger_fact/SurA_dom.
    [Graphical view ]
    Pfami PF00254. FKBP_C. 1 hit.
    PF05698. Trigger_C. 1 hit.
    PF05697. Trigger_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF003095. Trigger_factor. 1 hit.
    SUPFAMi SSF102735. SSF102735. 1 hit.
    SSF109998. SSF109998. 1 hit.
    TIGRFAMsi TIGR00115. tig. 1 hit.
    PROSITEi PS50059. FKBP_PPIASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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.

    Entry informationi

    Entry nameiTIG_ECOLI
    AccessioniPrimary (citable) accession number: P0A850
    Secondary accession number(s): P15299
    , P22257, P77603, Q2MBZ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: June 7, 2005
    Last modified: October 1, 2014
    This is version 95 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, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    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