TIG_ACICJ
ID TIG_ACICJ Reviewed; 440 AA.
AC A5FX03;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=Acry_0916;
OS Acidiphilium cryptum (strain JF-5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=349163;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF-5;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL Submitted (MAY-2007) 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; CP000697; ABQ30135.1; -; Genomic_DNA.
DR RefSeq; WP_007422420.1; NC_009484.1.
DR AlphaFoldDB; A5FX03; -.
DR SMR; A5FX03; -.
DR STRING; 349163.Acry_0916; -.
DR EnsemblBacteria; ABQ30135; ABQ30135; Acry_0916.
DR KEGG; acr:Acry_0916; -.
DR eggNOG; COG0544; Bacteria.
DR HOGENOM; CLU_033058_2_2_5; -.
DR OMA; KGIKTQF; -.
DR OrthoDB; 932993at2; -.
DR Proteomes; UP000000245; 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..440
FT /note="Trigger factor"
FT /id="PRO_1000022636"
FT DOMAIN 163..248
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00303"
SQ SEQUENCE 440 AA; 48760 MW; 6C7D7D2FE692B0B3 CRC64;
MQVTETLTEG LKRGFTVVVP GSDLSEKREK RLAELSKTMQ MPGFRPGKVP LSMVRKRFGD
AVAAEVMEAS VNEATERMIN DRSLRPAVQP KVEVVRAEPD SDLEFTVELE VLPEVTIPDL
KAISLTRPKA PVTEAEIDEA IARFAEQRAE TEVVTEDRPA ATGDILTVDF LGKRDGVPFE
GGAGTDTDIE LGGSGFIPGF AEQMEGMKAG ETKVITVTFP EQYHAAELAG KEATFDITAK
ALKRRVAPVI DDAFAEANGF ENLAEFRKFF ADRLEQSRAG ASRLKVKRAL LDKLAEQADF
PAPASLVDAE FAEIWRQVEA EKQAGRLDEE DAGKDEETLR ADYRAIAERR VRLGLLVAEI
GRTNNVQITE QDMRRAMIAE MQQFPGQEKM IMEFYQKNPR ALDRLRGPIF EDKVVDYALE
LATVTDEEVS AEALFADTDD
