ID   TIG_BACSU               Reviewed;         424 AA.
AC   P80698; P97173;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Trigger factor;
DE            Short=TF;
DE            EC=5.2.1.8;
DE   AltName: Full=PPIase;
DE   AltName: Full=Vegetative protein 2;
DE            Short=VEG2;
GN   Name=tig; Synonyms=yzzH; OrderedLocusNames=BSU28230;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, AND
RP   CHARACTERIZATION.
RX   PubMed=9063446; DOI=10.1111/j.1432-1033.1997.00059.x;
RA   Goethel S.F., Schmid R., Wipat A., Carter N.M., Emmerson P.T.,
RA   Harwood C.R., Marahiel M.A.;
RT   "An internal FK506-binding domain is the catalytic core of the prolyl
RT   isomerase activity associated with the Bacillus subtilis trigger factor.";
RL   Eur. J. Biochem. 244:59-65(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA   Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA   Emmerson P.T., Harwood C.R.;
RT   "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT   chromosome containing genes responsible for stress responses, the
RT   utilization of plant cell walls and primary metabolism.";
RL   Microbiology 142:3067-3078(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 217-408.
RA   Zouari N., Roche B., Seegers J.F.M.L., Seror S.J.;
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PROTEIN SEQUENCE OF 2-25.
RC   STRAIN=168 / IS58;
RX   PubMed=9084183; DOI=10.1099/00221287-143-3-991;
RA   Schmid R., Bernhardt J., Antelmann H., Voelker U., Mach H., Voelker A.,
RA   Hecker M.;
RT   "Identification of vegetative proteins for a two-dimensional protein index
RT   of Bacillus subtilis.";
RL   Microbiology 143:991-998(1997).
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; Z75208; CAA99536.1; -; Genomic_DNA.
DR   EMBL; Y09608; CAA70821.1; -; mRNA.
DR   EMBL; AL009126; CAB14783.1; -; Genomic_DNA.
DR   PIR; F69723; F69723.
DR   RefSeq; NP_390701.1; NC_000964.3.
DR   RefSeq; WP_003229611.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P80698; -.
DR   SMR; P80698; -.
DR   IntAct; P80698; 1.
DR   MINT; P80698; -.
DR   STRING; 224308.BSU28230; -.
DR   jPOST; P80698; -.
DR   PaxDb; P80698; -.
DR   PRIDE; P80698; -.
DR   EnsemblBacteria; CAB14783; CAB14783; BSU_28230.
DR   GeneID; 936610; -.
DR   KEGG; bsu:BSU28230; -.
DR   PATRIC; fig|224308.179.peg.3066; -.
DR   eggNOG; COG0544; Bacteria.
DR   InParanoid; P80698; -.
DR   OMA; KGIKTQF; -.
DR   PhylomeDB; P80698; -.
DR   BioCyc; BSUB:BSU28230-MON; -.
DR   Proteomes; UP000001570; Chromosome.
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: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; 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   1: Evidence at protein level;
KW   Cell cycle; Cell division; Chaperone; Cytoplasm; Direct protein sequencing;
KW   Isomerase; Reference proteome; Rotamase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9084183"
FT   CHAIN           2..424
FT                   /note="Trigger factor"
FT                   /id="PRO_0000179313"
FT   DOMAIN          163..248
FT                   /note="PPIase FKBP-type"
SQ   SEQUENCE   424 AA;  47487 MW;  D9A7B0D76661DAE2 CRC64;
     MSVKWEKQEG NEGVLTVEVD AETFKTALDD AFKKVVKQVS IPGFRKGKIP RGLFEQRFGV
     EALYQDALDI LLPVEYPKAV EEAGIEPVDR PEIDVEKIEK GESLIFTAKV TVKPEVKLGE
     YKGLGIEKDD TTVTDEDVQN ELKALQERQA ELVVKEEGAV EEGNTVVLDF EGFVDGEAFE
     GGKAENYSLE VGSGSFIPGF EDQLVGLEAG AEKDVEVTFP EEYHAEDLAG KPAVFKVKIH
     EIKAKELPEL DDEFAKDIDE EVETLAELTE KTKKRLEEAK ENEADAKLRE ELVLKASENA
     EIDVPQAMVD TELDRMLKEF EQRLQMQGMN LELYTQFSGQ DEAALKEQMK EDAEKRVKSN
     LTLEAIAKAE NLEVSDEEVD AELTKMAEAY NMPVENIKQA IGSTDAMKED LKVRKAIDFL
     VENR