ID   TIG_STAAE               Reviewed;         433 AA.
AC   A6QHK9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=NWMN_1569;
OS   Staphylococcus aureus (strain Newman).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=426430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Newman;
RX   PubMed=17951380; DOI=10.1128/jb.01000-07;
RA   Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT   "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT   analysis of staphylococcal genomes: polymorphism and evolution of two major
RT   pathogenicity islands.";
RL   J. Bacteriol. 190:300-310(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; AP009351; BAF67841.1; -; Genomic_DNA.
DR   RefSeq; WP_000127570.1; NZ_CP023390.1.
DR   AlphaFoldDB; A6QHK9; -.
DR   SMR; A6QHK9; -.
DR   EnsemblBacteria; BAF67841; BAF67841; NWMN_1569.
DR   KEGG; sae:NWMN_1569; -.
DR   HOGENOM; CLU_033058_3_2_9; -.
DR   OMA; KGIKTQF; -.
DR   Proteomes; UP000006386; 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..433
FT                   /note="Trigger factor"
FT                   /id="PRO_1000071989"
FT   DOMAIN          163..248
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00303"
SQ   SEQUENCE   433 AA;  48623 MW;  8865CB3F678BDEE7 CRC64;
     MTATWEKKEG NEGLLTVTVP AEKVNKALDQ AFKKVVKQIN VPGFRKGKVP RPIFEQRFGV
     EALYQDAIDI LLPDAYGEAI DETDIKPVAQ PEVSVTQIEK GKDFIFEATV TVEPEVKLGD
     YKGLEIEKQE TELSDDELQE AIDHSLGHLA EMVVKEDGVV ENGDTVNIDF SGSVDGEEFE
     GGQAEGYDLE IGSGSFIPGF EEQLEGMKVD EEKDVVVTFP EEYHAEELAG KEATFKTKVN
     EIKFKEVPEL TDEIANELDA EANTVDEYKE NLRKRLAEQK ATDAENVEKE EAITKATDNT
     TIDIPEAMIN TELDRMVSEF AQRIQQQGLD LQTYFQISGQ DETQLREQMK DDAEQRVKTN
     LTLTAIAEAE KIEATDEDID KELEKMSKQF NISVEDIKNT LGNTDIIKND VRIQKVIDLL
     RDNAKFVEGT KED