TIG_CAUVC
ID TIG_CAUVC Reviewed; 452 AA.
AC P0CAX0; O87705;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Trigger factor;
DE Short=TF;
DE EC=5.2.1.8;
DE AltName: Full=PPIase;
GN Name=tig; OrderedLocusNames=CC_1964;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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; AE005673; AAK23939.1; -; Genomic_DNA.
DR PIR; G87492; G87492.
DR RefSeq; NP_420771.1; NC_002696.2.
DR AlphaFoldDB; P0CAX0; -.
DR SMR; P0CAX0; -.
DR STRING; 190650.CC_1964; -.
DR EnsemblBacteria; AAK23939; AAK23939; CC_1964.
DR KEGG; ccr:CC_1964; -.
DR PATRIC; fig|190650.5.peg.1981; -.
DR eggNOG; COG0544; Bacteria.
DR HOGENOM; CLU_033058_2_2_5; -.
DR OMA; KGIKTQF; -.
DR BioCyc; CAULO:CC1964-MON; -.
DR Proteomes; UP000001816; 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..452
FT /note="Trigger factor"
FT /id="PRO_0000179331"
FT DOMAIN 169..254
FT /note="PPIase FKBP-type"
SQ SEQUENCE 452 AA; 49767 MW; 5C05DB6A4B2D4D94 CRC64;
MQIVEKSGEG LSRVFGVTVP ASELATRLEA RIAEVAPQMN VKGFRPGKVP TAHVRRLYGK
ALMGEVIEQA LNETTTKVLE DNKLRPAGQP ELNPSSDMDK VIAGGEDLSF DLAVEVMPEF
EPIDPTSIEL VKPVYKVSDE EVQEALDELA KQARTYEPRT GKSLKAKDGD QLLIDFVGTI
DGVEFAGGKA EGAELVLGSG QFIPGFEDQL VGAKPGDDVV VKVKFPEEYQ AKDLAGKDAE
FATKVQEVRA PVDGKADDEL AKRLGLSDLA ALTELLKSNL AGRYDNSSRF KLKRALLDVL
DTKHDFPLPP RMVDAEFAGI WQQVEADKAR GGLPPEDAEK TEDQLKDEYK KIAERRVRLG
LVLAEIGRKN DVVVTDQELT DAIMREARQY GAQAQQVFDM YRQRADLQAA LRAPIYEDKV
VDLIFGKAKI EEKEVSKDEL LEEDDLPEGY GG