TIG_KLEP7
ID TIG_KLEP7 Reviewed; 432 AA.
AC A6T5H9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
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};
GN OrderedLocusNames=KPN78578_03890; ORFNames=KPN_00398;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) 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; CP000647; ABR75850.1; -; Genomic_DNA.
DR RefSeq; WP_004147333.1; NC_009648.1.
DR AlphaFoldDB; A6T5H9; -.
DR BMRB; A6T5H9; -.
DR SMR; A6T5H9; -.
DR STRING; 272620.KPN_00398; -.
DR jPOST; A6T5H9; -.
DR EnsemblBacteria; ABR75850; ABR75850; KPN_00398.
DR KEGG; kpn:KPN_00398; -.
DR HOGENOM; CLU_033058_2_0_6; -.
DR OMA; KGIKTQF; -.
DR Proteomes; UP000000265; 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..432
FT /note="Trigger factor"
FT /id="PRO_1000022693"
FT DOMAIN 161..246
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00303"
SQ SEQUENCE 432 AA; 48113 MW; 730A665CC36FE441 CRC64;
MQVSVETTQG LGRRVTITIA ADSIENAVKS ELVNVAKKVR IDGFRKGKVP MNIVAQRYGA
SVRQDVLGDL MSRHFVDAII KEKINPAGAP NYVPGEYKLG EDFTYAVEFE VYPEVELQGL
DAIEVEKPVV EVTDADVDTM LETLRKQQAT WKEKEGAVDA EDRVTIDFTG SVDGEEFEGG
KASDFVLAMG QGRMIPGFED GIKGHKAGEE FTIDVTFPEE YHAENLKGKA AKFVINLKKV
EERELPELTE EFIKRFGVED GSVAGLRAEV RKNMERELKG AVRNRVKSQA IEGLVKANEI
DVPAALIDSE IDVLRRQAAQ RFGGNEKQAL ELPRELFEEQ AKRRVVVGLL LGEVIRTNEL
KADEERVKAL IEEMASAYED PSEVVEFYSK NKELMDNMRN VALEEQAVEA VLAKAKVSEK
ATSFNELMNQ QA
