ID   TIG_MYCPN               Reviewed;         444 AA.
AC   P75454; Q50352;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Trigger factor;
DE            Short=TF;
DE            EC=5.2.1.8;
DE   AltName: Full=PPIase;
GN   Name=tig; OrderedLocusNames=MPN_331; ORFNames=MP505;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 118-176.
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=7984111; DOI=10.1111/j.1365-2958.1994.tb00427.x;
RA   Proft T., Herrmann R.;
RT   "Identification and characterization of hitherto unknown Mycoplasma
RT   pneumoniae proteins.";
RL   Mol. Microbiol. 13:337-348(1994).
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; U00089; AAB96153.1; -; Genomic_DNA.
DR   EMBL; Z32656; CAA83577.1; -; Genomic_DNA.
DR   PIR; S73831; S73831.
DR   RefSeq; NP_110019.1; NC_000912.1.
DR   RefSeq; WP_010874687.1; NC_000912.1.
DR   AlphaFoldDB; P75454; -.
DR   SMR; P75454; -.
DR   IntAct; P75454; 4.
DR   STRING; 272634.MPN_331; -.
DR   EnsemblBacteria; AAB96153; AAB96153; MPN_331.
DR   KEGG; mpn:MPN_331; -.
DR   PATRIC; fig|272634.6.peg.355; -.
DR   HOGENOM; CLU_033058_3_2_14; -.
DR   OMA; KGIKTQF; -.
DR   BioCyc; MPNE272634:G1GJ3-524-MON; -.
DR   Proteomes; UP000000808; 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;
KW   Reference proteome; Rotamase.
FT   CHAIN           1..444
FT                   /note="Trigger factor"
FT                   /id="PRO_0000179388"
FT   DOMAIN          170..255
FT                   /note="PPIase FKBP-type"
SQ   SEQUENCE   444 AA;  51353 MW;  89475FDA4531FA82 CRC64;
     MKQYKLVNTT QKEKTLCLEI AIDTKLWKET QQKQTQDLTK NMKIKGFRKG KVPPTLAKDY
     LDRAELLQRS AQAVIDAIFQ PLQQEAVIAD NENVIEDFPT IDFKTINEND CVILFDFDLV
     PQFEPPDYKH IKDLSPIVPL KDEEFNKELH NIEKNKGKLV DVSDKALANN DIAVIDFVGK
     VDGKVLESAT AKQYELTIGS NSFIDGFESG LIGMKVGDKR QLKLKFPKDY HAEELKGKPV
     EFDIELKAIK QLEITPMDET NFKEYLPAQY QGFNSLKEFK TYFHKLVSAK KLEITLQENS
     VKIRQFFLAN TTLPYIPDSL IKLESDRLLR AQKDQAEQYK IPFERLLAAS KLSLEQLQQR
     NIKEARDNVT FALVMKRIAD VEKIKVDNKK IHSEIESIID VEYPFVNAEL KKQMFHNMEQ
     QKDFVESIIL NRLTTTKIIE YSTH