TIG_THEVB
ID TIG_THEVB Reviewed; 473 AA.
AC Q8DLI3;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Trigger factor {ECO:0000255|HAMAP-Rule:MF_00303};
DE Short=TF {ECO:0000255|HAMAP-Rule:MF_00303};
DE EC=5.2.1.8 {ECO:0000255|HAMAP-Rule:MF_00303};
DE AltName: Full=PPIase {ECO:0000255|HAMAP-Rule:MF_00303};
GN Name=tig {ECO:0000255|HAMAP-Rule:MF_00303}; OrderedLocusNames=tlr0508;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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. {ECO:0000255|HAMAP-
CC Rule:MF_00303}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00303};
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:0000255|HAMAP-Rule:MF_00303}.
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:0000255|HAMAP-Rule:MF_00303}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00303}.
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DR EMBL; BA000039; BAC08060.1; -; Genomic_DNA.
DR RefSeq; NP_681298.1; NC_004113.1.
DR AlphaFoldDB; Q8DLI3; -.
DR SMR; Q8DLI3; -.
DR STRING; 197221.22294229; -.
DR EnsemblBacteria; BAC08060; BAC08060; BAC08060.
DR KEGG; tel:tlr0508; -.
DR PATRIC; fig|197221.4.peg.535; -.
DR eggNOG; COG0544; Bacteria.
DR OMA; KGIKTQF; -.
DR OrthoDB; 932993at2; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Cell cycle; Cell division; Chaperone; Cytoplasm; Isomerase;
KW Reference proteome; Rotamase.
FT CHAIN 1..473
FT /note="Trigger factor"
FT /id="PRO_0000179447"
FT DOMAIN 167..251
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00303"
FT REGION 430..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 473 AA; 52880 MW; B2EA144CD130536D CRC64;
MTTEPRSNSQ LLATIEVSGT HSQQVYNQVV NDLLRHTQVP GFRKGKAPRQ LVLQQLGRER
LRYLAMEKLI EDAVKTAVEK NNIPYLGNLE LAGGITELLD QFHPGENFSF SVTFDVEPEV
TVTAYKGLTI EYNPVTYNPA TVEKLLQQHQ RQHATLIPVE DRPAQWGDDV TLKLLTKDEN
GEVVKELSAD ELPLSLDEDQ PFLLQEIPAA VVGMAIGEAK TVTVSVAEEA EAPRQLTAEI
ELLGIKVPEL PPLDDAFAAE HSEFSTMAEL RAYLEQNHQE RAKHQDKQAK EAALIDTLIA
QNPVELPKTL IRKEADVKVR TTLMQIQSQG VDLHKIMTEE LYERMRQEAE PAATKEVHSR
LLLKAIARQE GIEPTPEAVE ERLNRYKEML GNKTAKNLEQ LRKLAHDEVQ QEQTLSWLLE
QNTFQPVQSD VATAEPTATA EAPTEIQTEA VAQTPSQPQK RSGKKASSAP SQE
