ID   TIG_STRP6               Reviewed;         427 AA.
AC   Q5XA08; O85730;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   25-MAY-2022, entry version 91.
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=M6_Spy1620;
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HSC5 / Serotype M6;
RX   PubMed=9799235; DOI=10.1093/emboj/17.21.6263;
RA   Lyon W.R., Gibson C.M., Caparon M.G.;
RT   "A role for trigger factor and an rgg-like regulator in the transcription,
RT   secretion and processing of the cysteine proteinase of Streptococcus
RT   pyogenes.";
RL   EMBO J. 17:6263-6275(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-946 / MGAS10394;
RX   PubMed=15272401; DOI=10.1086/422697;
RA   Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA   Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT   "Progress toward characterization of the group A Streptococcus metagenome:
RT   complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL   J. Infect. Dis. 190:727-738(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAT87755.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF073922; AAC82391.1; -; Genomic_DNA.
DR   EMBL; CP000003; AAT87755.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011054989.1; NC_006086.1.
DR   AlphaFoldDB; Q5XA08; -.
DR   SMR; Q5XA08; -.
DR   EnsemblBacteria; AAT87755; AAT87755; M6_Spy1620.
DR   KEGG; spa:M6_Spy1620; -.
DR   HOGENOM; CLU_033058_3_2_9; -.
DR   Proteomes; UP000001167; 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..427
FT                   /note="Trigger factor"
FT                   /id="PRO_0000179442"
FT   DOMAIN          163..248
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00303"
SQ   SEQUENCE   427 AA;  47096 MW;  AD9E09B87C28450E CRC64;
     MSTSFENKAT NRGVITFTIS QDKIKPALDK AFNKIKKDLN APGFRKGHMP RPVFNQKFGE
     EVLYEDALNI VLPEAYEAAV TELGLDVVAQ PKIDVVSMEK GKEWTLSAEV VTKPEVKLGD
     YKNLVVEVDA SKEVSDEDVD AKIERERQNL AELIIKDGEA AQGDTVVIDF VGSVDGVEFD
     GGKGDNFSLE LGSGQFIPGF EDQLVGAKAG DEVEVNVTFP ESYQAEDLAG KAAKFMTTIH
     EVKTKEVPEL DDELAKDIDE DVDTLEDLKV KYRKELEAAQ ETAYDDAVEG AAIELAVANA
     EIVDLPEEMI HEEVNRSVNE FMGNMQRQGI SPEMYFQLTG TTQEDLHNQY SAEADKRVKT
     NLVIEAIAKA EGFEATDSEI EQEINDLATE YNMPADQVRS LLSADMLKHD IAMKKAVEVI
     TSTASVK