ID   TIG_PROM9               Reviewed;         481 AA.
AC   Q317Y7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=PMT9312_1747;
OS   Prochlorococcus marinus (strain MIT 9312).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9312;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000111; ABB50808.1; -; Genomic_DNA.
DR   RefSeq; WP_011377289.1; NC_007577.1.
DR   AlphaFoldDB; Q317Y7; -.
DR   SMR; Q317Y7; -.
DR   STRING; 74546.PMT9312_1747; -.
DR   EnsemblBacteria; ABB50808; ABB50808; PMT9312_1747.
DR   KEGG; pmi:PMT9312_1747; -.
DR   eggNOG; COG0544; Bacteria.
DR   HOGENOM; CLU_033058_3_1_3; -.
DR   OMA; KGIKTQF; -.
DR   OrthoDB; 932993at2; -.
DR   Proteomes; UP000002715; 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..481
FT                   /note="Trigger factor"
FT                   /id="PRO_0000256588"
FT   DOMAIN          174..261
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00303"
FT   REGION          435..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   481 AA;  53974 MW;  A171E89EB9971129 CRC64;
     MAKEALIVKT TPLPQSRISF ELEIPSETCK TCVNETISTI SRSAKIPGFR LGKIPKQVLI
     QRIGITQLHA SALEKIIDKS WQEALKIKSI EPLSEPELVD GFESLLAKFS PEKSLKFTLQ
     TDVAPELKLK KSKGLSVEIS KTKFDPKSVD EALEKSRSQF ANIIPVTNRA AKLGDIAVVS
     FKGKYKDSGK EIDGGTSESM DLELEKNKMI PGFVEGIVKM KIGDTKTLNL KFPEDYSHED
     SRGKEAIFEV SLKDLKEKEL PELNDDFAKQ SGNKESLKEL KKDIEKQLKE NFEKTQKDIK
     IEALLDALTN ELVAEIPKSM IDIEVRNNIE QTAQRFAQQG LDVKSTFTPE LVKSLSESTR
     PQAEKNVQRN LALKALAEKE NITVEKDEID LKMKDYEDAI SQSSKQIDIK KLTEVISKDL
     LKEKLIIWLE ENSEVKEKTT KASQASKTTK AKKTTTKTTK ATKTATKTTK ATKTQNKKEK
     K