ID E6TD23_MYCSR Unreviewed; 479 AA. AC E6TD23; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 27-MAR-2024, entry version 79. 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 OrderedLocusNames=Mspyr1_20210 {ECO:0000313|EMBL:ADT98675.1}; OS Mycolicibacterium gilvum (strain DSM 45189 / LMG 24558 / Spyr1) OS (Mycobacterium gilvum). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycolicibacterium. OX NCBI_TaxID=278137 {ECO:0000313|EMBL:ADT98675.1, ECO:0000313|Proteomes:UP000008916}; RN [1] {ECO:0000313|Proteomes:UP000008916} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45189 / LMG 24558 / Spyr1 RC {ECO:0000313|Proteomes:UP000008916}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., LaButti K., Ivanova N.M., Mikhailova N.M., Land M., Hauser L., RA Koukkou A.I., Drainas C., Kyrpides N., Woyke T.; RT "Complete sequence of chromosome of Mycobacterium sp. Spyr1."; RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADT98675.1, ECO:0000313|Proteomes:UP000008916} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45189 / LMG 24558 / Spyr1 RC {ECO:0000313|Proteomes:UP000008916}; RX PubMed=22180818; RA Kallimanis A., Karabika E., Mavromatis K., Lapidus A., Labutti K.M., RA Liolios K., Ivanova N., Goodwin L., Woyke T., Velentzas A.D., RA Perisynakis A., Ouzounis C.C., Kyrpides N.C., Koukkou A.I., Drainas C.; RT "Complete genome sequence of Mycobacterium sp. strain (Spyr1) and RT reclassification to Mycobacterium gilvum Spyr1."; RL Stand. Genomic Sci. 5:144-153(2011). 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:0000256|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; 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}. 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; CP002385; ADT98675.1; -; Genomic_DNA. DR RefSeq; WP_011893467.1; NC_014814.1. DR AlphaFoldDB; E6TD23; -. DR SMR; E6TD23; -. DR KEGG; msp:Mspyr1_20210; -. DR HOGENOM; CLU_033058_3_0_11; -. DR Proteomes; UP000008916; 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; 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|HAMAP-Rule:MF_00303, KW ECO:0000256|RuleBase:RU003914}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_00303, KW ECO:0000256|RuleBase:RU003914}; 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 Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|HAMAP-Rule:MF_00303}. FT DOMAIN 162..215 FT /note="PPIase FKBP-type" FT /evidence="ECO:0000259|PROSITE:PS50059" FT REGION 430..479 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 456..479 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 479 AA; 52361 MW; AA4AA3D4EABBE0EF CRC64; MKSTVEKLSP TRVRINVEVP FAELEPDIDK AFKQLAQQIR LPGFRPGKAP RKLLEARVGR GAVLEQVVND ALPTRYSQAV TSESLQPIGQ PEIEVTKLED NEELVFTAEV DVRPEIDLPD LSTLTITVDP VSVTDEDIEA EIEALQKRFG TLTGVERPAE NGDFVSIDLS ATVDGKDVPE AKTEGLSHEL GSGQLIEGLD EAIIGLSEDE SKTFTTTLVA GEHAGREAEV TVTVKSIKVR ELPELDDEFA QLASEFDTMD ELRADLREKV TRVKTVQQAE AIRDKAIEVL LEQTEVPLPE AVVQAQVDDT LHNAIHGLDH DEDRFADSLK EQGSSREEFD ADNRANAEKA IKTQLLMDAI ADKLEIQVGQ NDLSERLVLM SRQYGLEPQQ LLQMLQQNNQ LPAMFADVRR GLTVAAVVYA ATVTDTDGTE IDTTEFFGPS GDQAAAQQGA GEDDSEAAVE VSEDTADDAS EDDTADDTK //