TIG_DEIRA
ID TIG_DEIRA Reviewed; 465 AA.
AC Q9RT21;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Trigger factor;
DE Short=TF;
DE EC=5.2.1.8;
DE AltName: Full=PPIase;
GN Name=tig; OrderedLocusNames=DR_1948;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP PROTEIN SEQUENCE OF 2-16.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=15249204; DOI=10.1016/j.bbrc.2004.06.062;
RA Joshi B.S., Schmid R., Altendorf K., Apte S.K.;
RT "Protein recycling is a major component of post-irradiation recovery in
RT Deinococcus radiodurans strain R1.";
RL Biochem. Biophys. Res. Commun. 320:1112-1117(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1-114 IN COMPLEX WITH THE 50S
RP RIBOSOMAL SUBUNIT.
RX PubMed=16091460; DOI=10.1073/pnas.0505581102;
RA Baram D., Pyetan E., Sittner A., Auerbach-Nevo T., Bashan A., Yonath A.;
RT "Structure of trigger factor binding domain in biologically homologous
RT complex with eubacterial ribosome reveals its chaperone action.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12017-12022(2005).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 1-112 IN COMPLEX WITH THE 50S
RP RIBOSOMAL SUBUNIT.
RX PubMed=16271892; DOI=10.1016/j.str.2005.08.007;
RA Schluenzen F., Wilson D.N., Tian P., Harms J.M., McInnes S.J.,
RA Hansen H.A.S., Albrecht R., Buerger J., Wilbanks S.M., Fucini P.;
RT "The binding mode of the trigger factor on the ribosome: implications for
RT protein folding and SRP interaction.";
RL Structure 13:1685-1694(2005).
CC -!- FUNCTION: Involved in protein export. Acts as a chaperone by
CC maintaining the newly synthesized protein in an open conformation.
CC Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).
CC Probably changes conformation upon binding to the ribosome (maybe in
CC particular due to interaction with L24, PubMed:16271892), exposing a
CC hydrophobic crevice that is probably important for its chaperone
CC activity (PubMed:16091460 and PubMed:16271892). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC -!- SUBUNIT: Binds to the 50S ribosomal subunit via interactions with
CC ribosomal protein L23. Also interacts with 23S rRNA and proteins L24
CC and L29 when complexed with the ribosome (PubMed:16091460 and
CC PubMed:16271892). {ECO:0000269|PubMed:16091460,
CC ECO:0000269|PubMed:16271892}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=About half TF is bound to the
CC ribosome near the polypeptide exit tunnel while the other half is free
CC in the cytoplasm. {ECO:0000250}.
CC -!- DOMAIN: Consists of 3 domains; the N-terminus binds the ribosome, the
CC middle domain has PPIase activity, while the C-terminus has intrinsic
CC chaperone activity on its own. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily.
CC {ECO:0000305}.
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DR EMBL; AE000513; AAF11500.1; -; Genomic_DNA.
DR PIR; D75334; D75334.
DR RefSeq; NP_295671.1; NC_001263.1.
DR RefSeq; WP_010888581.1; NZ_CP015081.1.
DR PDB; 2AAR; X-ray; 3.50 A; 7=2-114.
DR PDB; 2D3O; X-ray; 3.35 A; 1=1-112.
DR PDBsum; 2AAR; -.
DR PDBsum; 2D3O; -.
DR AlphaFoldDB; Q9RT21; -.
DR SMR; Q9RT21; -.
DR STRING; 243230.DR_1948; -.
DR PRIDE; Q9RT21; -.
DR EnsemblBacteria; AAF11500; AAF11500; DR_1948.
DR KEGG; dra:DR_1948; -.
DR PATRIC; fig|243230.17.peg.2168; -.
DR eggNOG; COG0544; Bacteria.
DR HOGENOM; CLU_033058_3_1_0; -.
DR InParanoid; Q9RT21; -.
DR OMA; KGIKTQF; -.
DR OrthoDB; 932993at2; -.
DR EvolutionaryTrace; Q9RT21; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0043335; P:protein unfolding; IBA:GO_Central.
DR Gene3D; 1.10.3120.10; -; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 3.30.70.1050; -; 1.
DR HAMAP; MF_00303; Trigger_factor_Tig; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR005215; Trig_fac.
DR InterPro; IPR008880; Trigger_fac_C.
DR InterPro; IPR037041; Trigger_fac_C_sf.
DR InterPro; IPR008881; Trigger_fac_ribosome-bd_bac.
DR InterPro; IPR036611; Trigger_fac_ribosome-bd_sf.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR PANTHER; PTHR30560; PTHR30560; 1.
DR Pfam; PF05698; Trigger_C; 1.
DR Pfam; PF05697; Trigger_N; 1.
DR PIRSF; PIRSF003095; Trigger_factor; 1.
DR SUPFAM; SSF102735; SSF102735; 1.
DR SUPFAM; SSF109998; SSF109998; 1.
DR TIGRFAMs; TIGR00115; tig; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Chaperone; Cytoplasm;
KW Direct protein sequencing; Isomerase; Reference proteome; RNA-binding;
KW Rotamase; rRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15249204"
FT CHAIN 2..465
FT /note="Trigger factor"
FT /id="PRO_0000179344"
FT DOMAIN 160..235
FT /note="PPIase FKBP-type"
FT REGION 412..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:2D3O"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:2D3O"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:2D3O"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:2D3O"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:2D3O"
FT HELIX 63..81
FT /evidence="ECO:0007829|PDB:2D3O"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:2D3O"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:2D3O"
SQ SEQUENCE 465 AA; 51847 MW; 475E073690C8E006 CRC64;
MAELISKEGN KVEFKVSVPA AEVNRAYDQV WAGLARDVRV PGFRPGKAPR KVIENRVGKG
YVESQVRDRL LETHYSQGLR ELGLNLVDAT VDPQDVQSGQ AFEFTVKGET YPEVKLGDWQ
GLKVSAQAPE ITDEVLEQTL SDLRERNASF EKAERPIEAA DQVTIQELGE GDSEEGGSYP
IYLDMAEEHV RNALLGKSAG DVVDITVPAH QHGDHEHAEH TVRVKVVEVS SKKLQDLNDE
FATSLNYESM DKLRTDLREE LERRAQQEGD NLRREELVGH LVEGMTVEIP QALIDRRREG
MMSEIQDDLR RQGVQWKEYE AFMQEQGKLD EFEADLTKNA ETRVRRDLAL EQLATDLNAQ
VNEAEFNQTL MNLAQANGMN VQQLVQQLGQ DGVQSYYISL LRERGLQRAL AQLSGEGQST
EAASPKATGT EAAGTEQSEP AQTETAQNDA GQTETAQSEG EQQSE
