TIG_CERS5
ID TIG_CERS5 Reviewed; 444 AA.
AC A4WS82;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-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};
GN OrderedLocusNames=Rsph17025_1349;
OS Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=349102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17025 / ATH 2.4.3;
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 Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M.,
RA Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025.";
RL Submitted (APR-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000661; ABP70246.1; -; Genomic_DNA.
DR AlphaFoldDB; A4WS82; -.
DR SMR; A4WS82; -.
DR STRING; 349102.Rsph17025_1349; -.
DR EnsemblBacteria; ABP70246; ABP70246; Rsph17025_1349.
DR KEGG; rsq:Rsph17025_1349; -.
DR eggNOG; COG0544; Bacteria.
DR HOGENOM; CLU_033058_2_2_5; -.
DR OMA; KGIKTQF; -.
DR OrthoDB; 932993at2; -.
DR BioCyc; RSPH349102:G1G8M-1387-MON; -.
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..444
FT /note="Trigger factor"
FT /id="PRO_1000022743"
FT DOMAIN 166..251
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00303"
SQ SEQUENCE 444 AA; 49136 MW; 8A95C6604F9C9C0F CRC64;
MQVTETLKEG LKRAYTITVT AAELDAKVQE KLVEAQPDIE MKGFRKGKVP LAMLRKQFGP
RLLGDAMQDA IDGAMRDHLE TSGDRPAMQP EVRMVDGETW QEGTDVVVEM KYEALPEIPE
IETSKVTLER LVVKADEAAV DEALKNLAES AQNFDDRRKG SKAKDGDQIV IDFKGSVDGE
LFEGGSAEDY PLVLGSGSFI PGFEEQLVGA KVEDEVTVKV TFPTEYGAKH LAGKEAEFAC
TVKAVKAPKP AEIDDELAKK YGAEDLAALK AQIAERLEAE YKGASRAVLK RALLDQLDTM
VSFELPSKLV EAEAHQIAHQ LWHEEHPEEH GHNHGTIEPT DEHKALAERR VRLGLLLAEI
GRKAEVTVTD AEMTQAVLAQ ARQYPGQERA YFEFVQKNPQ IQQQLRAPIF EDKVVDLILE
GATVTEKEVG KDDLQKAIEA LDEM
