ID   TIG_MYCGE               Reviewed;         444 AA.
AC   P47480;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   04-NOV-2026, entry version 156.
DE   RecName: Full=Trigger factor;
DE            Short=TF;
DE            EC=5.2.1.8;
DE   AltName: Full=PPIase;
GN   Name=tig; OrderedLocusNames=MG238;
OS   Mycoplasmoides genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 /
OS   G37) (Mycoplasma genitalium).
OC   Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=243273;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA   Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA   Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA   Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA   Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA   Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA   Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT   "The minimal gene complement of Mycoplasma genitalium.";
RL   Science 270:397-403(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 141-216.
RC   STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX   PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA   Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT   "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL   J. Bacteriol. 175:7918-7930(1993).
RN   [3]
RP   STRUCTURE BY NMR OF 166-250.
RX   PubMed=12054805; DOI=10.1016/s0022-2836(02)00112-2;
RA   Vogtherr M., Jacobs D.M., Parac T.N., Maurer M., Pahl A., Saxena K.,
RA   Rueterjans H., Griesinger C., Fiebig K.M.;
RT   "NMR solution structure and dynamics of the peptidyl-prolyl cis-trans
RT   isomerase domain of the trigger factor from Mycoplasma genitalium compared
RT   to FK506-binding protein.";
RL   J. Mol. Biol. 318:1097-1115(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 (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; L43967; AAC71459.1; -; Genomic_DNA.
DR   EMBL; U01772; AAD10591.1; -; Genomic_DNA.
DR   PIR; C64226; C64226.
DR   RefSeq; WP_009885775.1; NC_000908.2.
DR   PDB; 1HXV; NMR; -; A=150-250.
DR   AlphaFoldDB; P47480; -.
DR   SMR; P47480; -.
DR   FunCoup; P47480; 210.
DR   STRING; 243273.MG_238; -.
DR   GeneID; 99647094; -.
DR   KEGG; mge:MG_238; -.
DR   eggNOG; COG0544; Bacteria.
DR   HOGENOM; CLU_033058_3_2_14; -.
DR   InParanoid; P47480; -.
DR   OMA; AACQVDI; -.
DR   OrthoDB; 9767721at2; -.
DR   BioCyc; MGEN243273:G1GJ2-285-MONOMER; -.
DR   EvolutionaryTrace; P47480; -.
DR   Proteomes; UP000000807; 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:0015031; P:protein transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0043335; P:protein unfolding; IBA:GO_Central.
DR   DisProt; DP01627; -.
DR   FunFam; 3.10.50.40:FF:000001; Trigger factor; 1.
DR   Gene3D; 3.10.50.40; -; 1.
DR   Gene3D; 3.30.70.1050; Trigger factor ribosome-binding domain; 1.
DR   Gene3D; 1.10.3120.10; Trigger factor, C-terminal domain; 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   NCBIfam; TIGR00115; tig; 1.
DR   PANTHER; PTHR30560; TRIGGER FACTOR CHAPERONE AND PEPTIDYL-PROLYL CIS/TRANS ISOMERASE; 1.
DR   PANTHER; PTHR30560:SF3; TRIGGER FACTOR-LIKE PROTEIN TIG, CHLOROPLASTIC; 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; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR   SUPFAM; SSF102735; Trigger factor ribosome-binding domain; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Chaperone; Cytoplasm; Isomerase;
KW   Reference proteome; Rotamase.
FT   CHAIN           1..444
FT                   /note="Trigger factor"
FT                   /id="PRO_0000179382"
FT   DOMAIN          170..255
FT                   /note="PPIase FKBP-type"
FT   STRAND          169..181
FT                   /evidence="ECO:0007829|PDB:1HXV"
FT   STRAND          192..198
FT                   /evidence="ECO:0007829|PDB:1HXV"
FT   HELIX           207..212
FT                   /evidence="ECO:0007829|PDB:1HXV"
FT   STRAND          216..222
FT                   /evidence="ECO:0007829|PDB:1HXV"
FT   STRAND          230..233
FT                   /evidence="ECO:0007829|PDB:1HXV"
FT   HELIX           234..236
FT                   /evidence="ECO:0007829|PDB:1HXV"
FT   STRAND          241..246
FT                   /evidence="ECO:0007829|PDB:1HXV"
SQ   SEQUENCE   444 AA;  50931 MW;  99704A2EA4E23F47 CRC64;
     MKLYKVLNSK TTDKSLCLEV EIDPNYWQAT QKKLVGEMAK SIKIKGFRPG KIPPNLASQS
     INKAELMQKS AQNVMNSIYE SVQQEEIVAS NDNVIDDYPT IDFKTITEQN CVLLFYFDLI
     PNFQLPDYKK IKDLTPLTKL TEAEFNNEIE KLAKTKSTMV DVSDKKLANG DIAIIDFTGI
     VDNKKLASAS AQNYELTIGS NSFIKGFETG LIAMKVNQKK TLALTFPSDY HVKELQSKPV
     TFEVVLKAIK KLEFTPMDET NFKSFLPEQF QSFTSLKAFK SYFHKLMENK KQETILQENN
     QKIRQFLLTN TKLPFLPEAL IKLEANRLLK LQQSQAEQYK IPFEKLLSAS NITLTELQDR
     NIKEAKENVT FALVMKKIAD IEKIKVDNNK IKAEIENVIA VEYPFASDEM KKQLFFNMEQ
     QKEFVESIII NRLTTTKIVS YSTH
//