TIG_CHLTR
ID TIG_CHLTR Reviewed; 442 AA.
AC O84713;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Trigger factor;
DE Short=TF;
DE EC=5.2.1.8;
DE AltName: Full=PPIase;
GN Name=tig; OrderedLocusNames=CT_707;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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; AE001273; AAC68302.1; -; Genomic_DNA.
DR PIR; D71481; D71481.
DR RefSeq; NP_220226.1; NC_000117.1.
DR RefSeq; WP_010725310.1; NC_000117.1.
DR AlphaFoldDB; O84713; -.
DR SMR; O84713; -.
DR STRING; 813.O172_03905; -.
DR EnsemblBacteria; AAC68302; AAC68302; CT_707.
DR GeneID; 884496; -.
DR KEGG; ctr:CT_707; -.
DR PATRIC; fig|272561.5.peg.778; -.
DR HOGENOM; CLU_065756_0_0_0; -.
DR InParanoid; O84713; -.
DR OMA; YTIEGFR; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0043335; P:protein unfolding; IBA:GO_Central.
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; 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; 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.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Chaperone; Cytoplasm; Isomerase;
KW Reference proteome; Rotamase.
FT CHAIN 1..442
FT /note="Trigger factor"
FT /id="PRO_0000179335"
FT DOMAIN 176..259
FT /note="PPIase FKBP-type"
SQ SEQUENCE 442 AA; 50101 MW; F3EED2D8F1CCE313 CRC64;
MSSRDFSNDL FSINIEENAG CVVSAKVQAN PLVTQKCHKE ALKTVKKNVV LPGFRKGKAP
DNIVESRYST QMEQELRRLF LRASFEALSQ MCDRKPLSPK AVRSSAIDTC NPVNGGSVSF
LYEAFPVIPS LPWEQLSLPD PEPVKEISEE DLENGLKNVA YFFATKTPVT RPSQEGDFIS
LSLYVSKRGD ENSTPVAIFE NKYFKISEED MTDSFKARFL NVSTGHRVEE EIGSEDIQSF
LNGDLLTFTV NAVIEISSPE MDDEKARQLQ AESLEDLKKK LRIQLENQAK EAQHQKRFSD
AEDALAQLID FDLPESLLQE REELLSREKL LNARLVKYCS DSELEEQKQA LLEEAKADAR
KAVKLLFLTQ KVFSEKGLSI SREELQYMMD VCSRERFGGY PPKDISNEMI QELVLVARDR
LTYRKAIEAI SSEKKDLEVV PS