ID   TIG_AYWBP               Reviewed;         431 AA.
AC   Q2NJE2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=AYWB_334;
OS   Aster yellows witches'-broom phytoplasma (strain AYWB).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX   NCBI_TaxID=322098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AYWB;
RX   PubMed=16672622; DOI=10.1128/jb.188.10.3682-3696.2006;
RA   Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A., Shevchenko D.V.,
RA   Tsukerman K., Walunas T., Lapidus A., Campbell J.W., Hogenhout S.A.;
RT   "Living with genome instability: the adaptation of phytoplasmas to diverse
RT   environments of their insect and plant hosts.";
RL   J. Bacteriol. 188:3682-3696(2006).
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; CP000061; ABC65451.1; -; Genomic_DNA.
DR   RefSeq; WP_011412615.1; NC_007716.1.
DR   AlphaFoldDB; Q2NJE2; -.
DR   SMR; Q2NJE2; -.
DR   STRING; 322098.AYWB_334; -.
DR   EnsemblBacteria; ABC65451; ABC65451; AYWB_334.
DR   KEGG; ayw:AYWB_334; -.
DR   eggNOG; COG0544; Bacteria.
DR   HOGENOM; CLU_033058_3_2_14; -.
DR   OMA; KGIKTQF; -.
DR   OrthoDB; 932993at2; -.
DR   PhylomeDB; Q2NJE2; -.
DR   Proteomes; UP000001934; 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; 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.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Chaperone; Cytoplasm; Isomerase; Rotamase.
FT   CHAIN           1..431
FT                   /note="Trigger factor"
FT                   /id="PRO_0000256529"
FT   DOMAIN          165..250
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00303"
SQ   SEQUENCE   431 AA;  50267 MW;  91C67CCD4BD3D7FE CRC64;
     MKIKKINNQK VQYFFKVSSK ELETQLSSAY EKIKSKVEIK GFRKGHVPRK IFENHFGKNN
     LYSDALENIV QTKYQEILQK KDFESMGMPQ VIDLNEKKLK DNQNFTFGLE FIVKPKVILK
     KYLGLEITKD ELEVKDCEVE EKINSLLEKQ ATLESKTQNN SLELTDTAVF DFEGFVDEKP
     FEGGTAKNFS LKIGSGQFLP GFEDQMLGMK QGQNKDINIT FPSDYHQKKL ANKKVIFKVT
     LHQIKTKKIP QLTDNLVKLL KLANVSTVEE LKNNTKKTLL DQKKHKEKEN IKKQVIEQLV
     KNSELQIPQE IISQEKTHLQ KEFEKQLKQQ NLTLEQYKQY LGIGDEKMEK EFNQQAQKNL
     QYRLIIEQVA FQEKLTISKE KIEQQYKNLS NHYKVPVNQI KQNLPEKNLQ HSLLMDEALD
     LVINKAVVVT K