ID A0A1W1W8P6_SULTA Unreviewed; 438 AA.
AC A0A1W1W8P6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Trigger factor {ECO:0000256|HAMAP-Rule:MF_00303, ECO:0000256|RuleBase:RU003914};
DE Short=TF {ECO:0000256|HAMAP-Rule:MF_00303};
DE EC=5.2.1.8 {ECO:0000256|HAMAP-Rule:MF_00303};
DE AltName: Full=PPIase {ECO:0000256|HAMAP-Rule:MF_00303};
GN Name=tig {ECO:0000256|HAMAP-Rule:MF_00303};
GN ORFNames=SAMN00768000_0704 {ECO:0000313|EMBL:SMC02667.1};
OS Sulfobacillus thermosulfidooxidans (strain DSM 9293 / VKM B-1269 / AT-1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Clostridiales Family XVII. Incertae Sedis; Sulfobacillus.
OX NCBI_TaxID=929705 {ECO:0000313|EMBL:SMC02667.1, ECO:0000313|Proteomes:UP000192660};
RN [1] {ECO:0000313|Proteomes:UP000192660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9293 {ECO:0000313|Proteomes:UP000192660};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) 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.
CC {ECO:0000256|ARBA:ARBA00024849, ECO:0000256|HAMAP-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;
CC Evidence={ECO:0000256|ARBA:ARBA00000971, ECO:0000256|HAMAP-
CC Rule:MF_00303, ECO:0000256|PROSITE-ProRule:PRU00277};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00303}.
CC Note=About half TF is bound to the ribosome near the polypeptide exit
CC tunnel while the other half is free in the cytoplasm.
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_00303}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. Tig subfamily.
CC {ECO:0000256|ARBA:ARBA00005464, ECO:0000256|HAMAP-Rule:MF_00303,
CC ECO:0000256|RuleBase:RU003914}.
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DR EMBL; FWWY01000001; SMC02667.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1W8P6; -.
DR STRING; 28034.BFX07_05080; -.
DR OrthoDB; 9767721at2; -.
DR Proteomes; UP000192660; Unassembled WGS sequence.
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; 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; 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 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; PF00254; FKBP_C; 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.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_00303};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_00303};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00303};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00303};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00303};
KW Reference proteome {ECO:0000313|Proteomes:UP000192660};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|HAMAP-Rule:MF_00303}.
FT DOMAIN 164..221
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 438 AA; 48670 MW; 3FCECF174D49D959 CRC64;
MQVALQRLPN SVAKVSVTID PSDLSKAMDK AFRNVVGKYN IPGFRRGKVP RPIFERFVGR
EVILQEAAQQ LVENRYYEAL SEVSVEPVAE PKINIVKLDD GQPFEFDIEV ESKPQIDLPD
YQDLLQEPLE IPVPTDEQID AELALVAKGQ AQIVPADDEP VAKGNRIVVS LKGFLDDGED
DSEPFVDDDA YTIEVGAGTV VEGLEDQLVG LKVNEPQVIK LTYPENHPDV SLAGKPVRFE
LTVVENKRPD IPEVNDDLAK AVGLESLQEL REQVTNNLKT RLEEQAKNAR LQTILGKLKE
RVSVEVPSAL VDQAIHNQLH ELENTLARIG ASTQEYLESR QITPEALHDE LRPAAEERVK
EELLLEAIAK QQGFEVSDEE VIQAIKPVAD MYRQPLSDMV RLFRSSGEFE ALRTNILLSK
ASTYLASTVA GGQGESEQ
//
