FKBPL_METJA
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 25-MAY-2022, entry version 111.
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}.
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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 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 OMA; IREFHRH; -.
DR OrthoDB; 116879at2157; -.
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 Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR040825; FKBP26_C.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR Pfam; PF18046; FKBP26_C; 1.
DR Pfam; PF00254; FKBP_C; 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
