FKBPS_METJA
ID FKBPS_METJA Reviewed; 157 AA.
AC Q57726;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Short-type peptidyl-prolyl cis-trans isomerase {ECO:0000250|UniProtKB:O52980};
DE Short=Short-type PPIase {ECO:0000250|UniProtKB:O52980};
DE EC=5.2.1.8 {ECO:0000250|UniProtKB:O52980};
DE AltName: Full=FKBP-type peptidyl-prolyl cis-trans isomerase {ECO:0000250|UniProtKB:O52980};
DE Short=FKBP-type PPIase {ECO:0000250|UniProtKB:O52980};
DE AltName: Full=Rotamase;
GN OrderedLocusNames=MJ0278;
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).
CC -!- FUNCTION: Catalyzes the cis-trans isomerization of peptidyl prolyl
CC bonds and accelerates protein folding. Also exhibits chaperone-like
CC activity. {ECO:0000250|UniProtKB:O52980}.
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:O52980};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O52980}.
CC -!- DOMAIN: Contains an N-terminal PPIase domain and an IF (Insert in the
CC Flap) domain. {ECO:0000250|UniProtKB:O52980}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR EMBL; L77117; AAB98266.1; -; Genomic_DNA.
DR PIR; G64334; G64334.
DR AlphaFoldDB; Q57726; -.
DR SMR; Q57726; -.
DR STRING; 243232.MJ_0278; -.
DR EnsemblBacteria; AAB98266; AAB98266; MJ_0278.
DR KEGG; mja:MJ_0278; -.
DR eggNOG; arCOG00981; Archaea.
DR HOGENOM; CLU_098197_2_0_2; -.
DR InParanoid; Q57726; -.
DR OMA; HSHEGGC; -.
DR PhylomeDB; Q57726; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 3: Inferred from homology;
KW Chaperone; Cytoplasm; Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..157
FT /note="Short-type peptidyl-prolyl cis-trans isomerase"
FT /id="PRO_0000075376"
FT DOMAIN 1..95
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REGION 86..137
FT /note="IF"
FT /evidence="ECO:0000250|UniProtKB:Q58235"
SQ SEQUENCE 157 AA; 17680 MW; 36C895C541FA0D44 CRC64;
MINLIKKGDY VKVDYILEVD GKVIDTSIEE VAKENKIYYP EREYEPIGFI VGNGELIEGF
EEAVIGMEVG EEKTVTIPPE KGYGLRDERL IQEIPKEMFA DADFEPQEGM LILASGIPAK
IIKVTDDTVT LDFNHELAGK ELKFTIKVRD VQPAESE
