ID FKBPL_METJA Reviewed; 231 AA. AC Q58235; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 27-MAR-2024, entry version 115. DE RecName: Full=Long-type peptidyl-prolyl cis-trans isomerase {ECO:0000305}; DE Short=Long-type PPIase {ECO:0000305}; DE EC=5.2.1.8 {ECO:0000250|UniProtKB:O27197}; DE AltName: Full=FKBP-type peptidyl-prolyl cis-trans isomerase {ECO:0000305}; DE Short=FKBP-type PPIase {ECO:0000305}; DE AltName: Full=FKBP26 {ECO:0000303|PubMed:21262232}; DE AltName: Full=Rotamase {ECO:0000305}; GN OrderedLocusNames=MJ0825; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM OS 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L., RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] {ECO:0007744|PDB:3PR9, ECO:0007744|PDB:3PRA, ECO:0007744|PDB:3PRB, ECO:0007744|PDB:3PRD} RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-150, FUNCTION AS A CHAPERONE, RP SUBUNIT, AND DOMAIN. RX PubMed=21262232; DOI=10.1016/j.jmb.2011.01.027; RA Martinez-Hackert E., Hendrickson W.A.; RT "Structural analysis of protein folding by the long-chain archaeal RT chaperone FKBP26."; RL J. Mol. Biol. 407:450-464(2011). CC -!- FUNCTION: Catalyzes the cis-trans isomerization of peptidyl prolyl CC bonds and accelerates protein folding (By similarity). Also exhibits CC chaperone-like activity (PubMed:21262232). CC {ECO:0000250|UniProtKB:O27197, ECO:0000269|PubMed:21262232}. 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:0000250|UniProtKB:O27197}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21262232}. CC -!- DOMAIN: Contains an N-terminal PPIase domain, an IF (Insert in the CC Flap) domain and a C-terminal domain (CTD). The CTD mediates CC dimerization. Chaperone activity requires both the IF domain and the CC CTD. {ECO:0000269|PubMed:21262232}. CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}. 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; L77117; AAB98824.1; -; Genomic_DNA. DR RefSeq; WP_010870336.1; NC_000909.1. DR PDB; 3PR9; X-ray; 1.95 A; A=1-150. DR PDB; 3PRA; X-ray; 2.40 A; A/B=1-150. DR PDB; 3PRB; X-ray; 2.20 A; A/B=1-231. DR PDB; 3PRD; X-ray; 3.30 A; A=1-231. DR PDBsum; 3PR9; -. DR PDBsum; 3PRA; -. DR PDBsum; 3PRB; -. DR PDBsum; 3PRD; -. DR AlphaFoldDB; Q58235; -. DR SMR; Q58235; -. DR STRING; 243232.MJ_0825; -. DR PaxDb; 243232-MJ_0825; -. DR EnsemblBacteria; AAB98824; AAB98824; MJ_0825. DR GeneID; 1451708; -. DR KEGG; mja:MJ_0825; -. DR eggNOG; arCOG00980; Archaea. DR HOGENOM; CLU_073526_1_0_2; -. DR InParanoid; Q58235; -. DR OrthoDB; 8615at2157; -. DR PhylomeDB; Q58235; -. DR EvolutionaryTrace; Q58235; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt. DR Gene3D; 2.40.10.330; -; 1. DR Gene3D; 3.10.50.40; -; 1. DR Gene3D; 3.30.70.2210; -; 1. DR InterPro; IPR040825; FKBP26_C. DR InterPro; IPR046357; PPIase_dom_sf. DR InterPro; IPR001179; PPIase_FKBP_dom. DR InterPro; IPR048261; SlpA/SlyD-like_ins_sf. DR PANTHER; PTHR47861; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE SLYD; 1. DR PANTHER; PTHR47861:SF2; LONG-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1. DR Pfam; PF18046; FKBP26_C; 1. DR Pfam; PF00254; FKBP_C; 1. DR SUPFAM; SSF54534; FKBP-like; 1. DR PROSITE; PS50059; FKBP_PPIASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Chaperone; Isomerase; Reference proteome; Rotamase. FT CHAIN 1..231 FT /note="Long-type peptidyl-prolyl cis-trans isomerase" FT /id="PRO_0000075377" FT DOMAIN 5..92 FT /note="PPIase FKBP-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277" FT REGION 83..134 FT /note="IF" FT /evidence="ECO:0000305|PubMed:21262232" FT REGION 151..231 FT /note="CTD" FT /evidence="ECO:0000305|PubMed:21262232" FT STRAND 7..16 FT /evidence="ECO:0007829|PDB:3PR9" FT STRAND 19..24 FT /evidence="ECO:0007829|PDB:3PR9" FT HELIX 26..31 FT /evidence="ECO:0007829|PDB:3PR9" FT STRAND 44..47 FT /evidence="ECO:0007829|PDB:3PR9" FT STRAND 50..53 FT /evidence="ECO:0007829|PDB:3PR9" FT HELIX 55..63 FT /evidence="ECO:0007829|PDB:3PR9" FT STRAND 69..74 FT /evidence="ECO:0007829|PDB:3PR9" FT HELIX 76..78 FT /evidence="ECO:0007829|PDB:3PR9" FT HELIX 85..87 FT /evidence="ECO:0007829|PDB:3PR9" FT STRAND 88..92 FT /evidence="ECO:0007829|PDB:3PR9" FT HELIX 93..98 FT /evidence="ECO:0007829|PDB:3PR9" FT STRAND 108..111 FT /evidence="ECO:0007829|PDB:3PR9" FT STRAND 114..122 FT /evidence="ECO:0007829|PDB:3PR9" FT STRAND 125..129 FT /evidence="ECO:0007829|PDB:3PR9" FT TURN 133..136 FT /evidence="ECO:0007829|PDB:3PR9" FT STRAND 139..149 FT /evidence="ECO:0007829|PDB:3PR9" FT HELIX 152..163 FT /evidence="ECO:0007829|PDB:3PRB" FT STRAND 171..175 FT /evidence="ECO:0007829|PDB:3PRB" FT STRAND 178..182 FT /evidence="ECO:0007829|PDB:3PRB" FT HELIX 187..189 FT /evidence="ECO:0007829|PDB:3PRB" FT HELIX 193..207 FT /evidence="ECO:0007829|PDB:3PRB" FT STRAND 213..221 FT /evidence="ECO:0007829|PDB:3PRB" SQ SEQUENCE 231 AA; 25947 MW; ABD9AD1DB1B6C420 CRC64; MVEKGKMVKI SYDGYVDGKL FDTTNEELAK KEGIYNPAMI YGPVAIFAGE GQVLPGLDEA ILEMDVGEER EVVLPPEKAF GKRDPSKIKL IPLSEFTKRG IKPIKGLTIT IDGIPGKIVS INSGRVLVDF NHELAGKEVK YRIKIEEVVD DKKNIVKEIV KMYVPRLSDV KVTIRNGTVK IELPEFAPFI PNIQTAKMAI ANEILKRLED AEKVSFVETF ERKKETKEEN K //