TIG_MYCGE
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 03-AUG-2022, entry version 140.
DE RecName: Full=Trigger factor;
DE Short=TF;
DE EC=5.2.1.8;
DE AltName: Full=PPIase;
GN Name=tig; OrderedLocusNames=MG238;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
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; NZ_AAGX01000005.1.
DR PDB; 1HXV; NMR; -; A=150-250.
DR PDBsum; 1HXV; -.
DR AlphaFoldDB; P47480; -.
DR SMR; P47480; -.
DR STRING; 243273.MG_238; -.
DR EnsemblBacteria; AAC71459; AAC71459; MG_238.
DR KEGG; mge:MG_238; -.
DR eggNOG; COG0544; Bacteria.
DR HOGENOM; CLU_033058_3_2_14; -.
DR OMA; KGIKTQF; -.
DR OrthoDB; 932993at2; -.
DR BioCyc; MGEN243273:G1GJ2-285-MON; -.
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: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 DisProt; DP01627; -.
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 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
