ID A0A6L4V528_9BIFI Unreviewed; 453 AA. AC A0A6L4V528; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 03-MAY-2023, entry version 11. 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=GBA80_03790 {ECO:0000313|EMBL:KAB7464126.1}; OS Bifidobacterium catenulatum. OC Bacteria; Actinomycetota; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=1686 {ECO:0000313|EMBL:KAB7464126.1, ECO:0000313|Proteomes:UP000480423}; RN [1] {ECO:0000313|EMBL:KAB7464126.1, ECO:0000313|Proteomes:UP000480423} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BIOML-A1 {ECO:0000313|EMBL:KAB7464126.1, RC ECO:0000313|Proteomes:UP000480423}; RX PubMed=31477907; DOI=.1038/s41591-019-0559-3; RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X., RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D., RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J., RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A., RA Xavier R.J., Alm E.J.; RT "A library of human gut bacterial isolates paired with longitudinal RT multiomics data enables mechanistic microbiome research."; RL Nat. Med. 25:1442-1452(2019). 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KAB7464126.1}. 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; WDPA01000002; KAB7464126.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6L4V528; -. DR Proteomes; UP000480423; 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 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 TIGRFAMs; TIGR00115; tig; 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 166..213 FT /note="PPIase FKBP-type" FT /evidence="ECO:0000259|PROSITE:PS50059" SQ SEQUENCE 453 AA; 48974 MW; 383FFF55956421A9 CRC64; MKISVRNLEP TKVRLTVTVD PEEFNPYLDN ARKEIAKQVN VPGFRKGHVP GKIIDQRIGF GAVAGEAVNN GVPELYSKAL EEKGIHPMAQ PEIDVQEVPE SAKDETKLKF VATVERRPDI ELPAIDGMEI EVAKAEITDE DINNRLEALR QRFGTLVGVD RPAAKGDYAN IDLTAEIDGE VVDSQEGVSY ELGSETMLDG LDEALEGLSS GEETTFEGTL EAGEHEGEKA QVKVKVNSVK AEELPELDDD FASEASEFDT LDELKEDLKK AASQDAEGRQ ATAARDAFIA KLEEGLEIPV PKGVKAEMVE QQLKGVTADP DNATKEQKAE AEETVEKELR DQMVLDVLAE KLDIKVSQAD VFNFLASIAQ QYGMDPNAFI QAIMRNGQLG SAVQEVGRSK GLLAGMRAVA FKSEGETLDL SAFLGEAAED EEAESVEAAS AAAAVADELA SEE //