ID   TIG_KOCRD               Reviewed;         448 AA.
AC   B2GGB4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
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=KRH_11070;
OS   Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Kocuria.
OX   NCBI_TaxID=378753;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201;
RX   PubMed=18408034; DOI=10.1128/jb.01853-07;
RA   Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA   Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL   J. Bacteriol. 190:4139-4146(2008).
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; AP009152; BAG29454.1; -; Genomic_DNA.
DR   RefSeq; WP_012398175.1; NZ_VECX01000005.1.
DR   AlphaFoldDB; B2GGB4; -.
DR   SMR; B2GGB4; -.
DR   STRING; 378753.KRH_11070; -.
DR   PRIDE; B2GGB4; -.
DR   EnsemblBacteria; BAG29454; BAG29454; KRH_11070.
DR   KEGG; krh:KRH_11070; -.
DR   eggNOG; COG0544; Bacteria.
DR   HOGENOM; CLU_033058_3_0_11; -.
DR   OMA; KGIKTQF; -.
DR   OrthoDB; 932993at2; -.
DR   Proteomes; UP000008838; 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..448
FT                   /note="Trigger factor"
FT                   /id="PRO_1000115545"
FT   DOMAIN          166..245
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00303"
FT   REGION          314..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          424..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..448
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   448 AA;  48943 MW;  F17B76B05DB0D7D1 CRC64;
     MKSAVEKLNP TEAKITIDIA YTDLKPFVQE TYKELANQIQ IPGFRKGKVP SKLIDQRVGF
     DFVVENALNE GLNAFYQQAL TENELTPLSQ PQVEVLSKPE ENDREADTKV EISVAIRPEI
     ELPDYKGLEI QVEAREATAE DEQKALDELR ARFGTLKTVD RPAAEGDHVT LDLQALVDGE
     EVDAANDLSY EVGSGTMLEG IDEAVTGLSA GEDATFETTL AGGEHSGAEA TVKVKVTAVK
     ERELPEADDE FAQLASEFDT IAELKEDLKK QAAESAVVEQ GIEARDKVLD KLVELIEVPV
     PEKVIEDQLA QHFDSEQAQA SAEPGHDTEE HRAEVRQNAE NAFRNEIILD AVAEAEEVGV
     EQSELIDYII NMSQQYGMDP NQFAQMLDGS GQAGMMVGEV RRRKALAKVL ETATVTDSNG
     ETVDLSSFVG TGDDAETDEV ETEASATE