ID TIG_RHOBA Reviewed; 480 AA.
AC Q7URG5;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 13-SEP-2023, entry version 96.
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=RB5681;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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 -!- SEQUENCE CAUTION:
CC Sequence=CAD74375.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX294142; CAD74375.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_866834.1; NC_005027.1.
DR AlphaFoldDB; Q7URG5; -.
DR SMR; Q7URG5; -.
DR STRING; 243090.RB5681; -.
DR EnsemblBacteria; CAD74375; CAD74375; RB5681.
DR KEGG; rba:RB5681; -.
DR PATRIC; fig|243090.15.peg.2728; -.
DR eggNOG; COG0544; Bacteria.
DR HOGENOM; CLU_033058_3_3_0; -.
DR InParanoid; Q7URG5; -.
DR OrthoDB; 9767721at2; -.
DR Proteomes; UP000001025; 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; 3.10.50.40; -; 1.
DR Gene3D; 3.30.70.1050; Trigger factor ribosome-binding domain; 1.
DR Gene3D; 1.10.3120.10; Trigger factor, C-terminal domain; 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 NCBIfam; TIGR00115; tig; 1.
DR PANTHER; PTHR30560; TRIGGER FACTOR CHAPERONE AND PEPTIDYL-PROLYL CIS/TRANS ISOMERASE; 1.
DR PANTHER; PTHR30560:SF3; TRIGGER FACTOR-LIKE PROTEIN TIG, CHLOROPLASTIC; 1.
DR Pfam; PF05698; Trigger_C; 1.
DR Pfam; PF05697; Trigger_N; 1.
DR PIRSF; PIRSF003095; Trigger_factor; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR SUPFAM; SSF102735; Trigger factor ribosome-binding domain; 1.
PE 3: Inferred from homology;
KW Cell cycle; Cell division; Chaperone; Cytoplasm; Isomerase;
KW Reference proteome; Rotamase.
FT CHAIN 1..480
FT /note="Trigger factor"
FT /id="PRO_0000179413"
FT DOMAIN 161..249
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00303"
FT REGION 426..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 480 AA; 54874 MW; EE9FF5E8CA93447B CRC64;
MEVTKPHACL REVVVTIPRG EVDRYMKDAY DELVPEAQVP GFRAGRAPRK LVEKQFKDRI
EDRVKGSLLM DSLAKVTEDA EFSAIGEPDF DYESIELPEK GEFKYQFSIE VRPEFETPDW
KKLELKKPVE TISEEDVDAA LQRVLSRYAS LEASDAPAEI GDRLLITGKF VDGEKTISEM
DEERVTLANR LSLSDAVCEN FGELMKDCKE GDVVTGKVKL GEGHANEEMQ GKEVDATFTV
VEVLKEQLPE LTSEFLDELG EFETEDELRE FVRASLERQA NFRTEQAMRG SIIEKLLASA
DFELPPTLVR RQMKRELDRK VLEFRRSGFD DDMIRRFVNA SKQNMQQGTE SSLREHFILE
QIADEEKIDA EPQEYETEIQ LIAEQSDSSP RRVRARLEKT GQMDALRNQI VERKVIELIS
EAATVTEEPV EKEAEEKNEE FAIDHEVLPT KDHDAIPAAK YDDNTPKGAE TEDKQEKDKD
//
