ID   TIG_AZOBR               Reviewed;         444 AA.
AC   Q9X6W7;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Trigger factor;
DE            Short=TF;
DE            EC=5.2.1.8;
DE   AltName: Full=PPIase;
GN   Name=tig;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SpF94;
RA   Indorato C., Giannelli L., Bazzicalupo M.;
RT   "Azospirillum brasilense tig-clp-clpx-lon.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
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       {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   -!- 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; AF150957; AAD37434.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9X6W7; -.
DR   SMR; Q9X6W7; -.
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; IPR001179; PPIase_FKBP_dom.
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; PF00254; FKBP_C; 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; Rotamase.
FT   CHAIN           1..444
FT                   /note="Trigger factor"
FT                   /id="PRO_0000179303"
FT   DOMAIN          163..248
FT                   /note="PPIase FKBP-type"
SQ   SEQUENCE   444 AA;  49408 MW;  67315088541C1121 CRC64;
     MNITETSADG LKREYKVVIS AQDIEQKVQG RLEELRRTVQ LPGFRPGKVP VAVIKQRYGG
     SVLAEALEDA IADSSRQALN ERGLRIAMQP KINVEKYEDG GDLSYTMGVE LLPDIEPGDL
     SGLELEKPVA TVEDSAVDEA LTRLASAHSV QAPVTEDRAA EKGDIAVIDS PVRSTGEALP
     GMDGKDYPLE LGANQFVPGF EDQLVGAKAG EHRTVKVTFP ADYPHDRLKG ADTVFEVDVK
     ELRKNVPAEV NDDLAKEFGM ESLEKLREAV GRPHQGRIRQ RVALRVKRQL LDKLAEAHSF
     EVPPGMVDVE FEGIWQRLQQ ELQNGTAGED AGKPEEELKT EYRGIAERRV RLGLLLSEIG
     RRNDIQVTQD EINRALIAEA RRFPGQERQV FEFFKQNREA LENLRAPIFE DKVVDYILDQ
     AKVSEKPVSA EELMKDPDEE AEAA