ID   FKBPS_METTL             Reviewed;         151 AA.
AC   O52980;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2020, sequence version 2.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Short-type peptidyl-prolyl cis-trans isomerase {ECO:0000305};
DE            Short=Short-type PPIase {ECO:0000305};
DE            EC=5.2.1.8 {ECO:0000269|PubMed:10631007, ECO:0000269|PubMed:9440528};
DE   AltName: Full=FKBP-type peptidyl-prolyl cis-trans isomerase {ECO:0000305};
DE            Short=FKBP-type PPIase {ECO:0000303|PubMed:9440528};
DE   AltName: Full=MTFK {ECO:0000303|PubMed:9440528};
DE   AltName: Full=Rotamase;
OS   Methanothermococcus thermolithotrophicus (Methanococcus
OS   thermolithotrophicus).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanothermococcus.
OX   NCBI_TaxID=2186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-28; 79-98 AND
RP   138-145, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 35097 / DSM 2095 / JCM 10549 / OCM 138 / SN-1;
RX   PubMed=9440528; DOI=10.1128/jb.180.2.388-394.1998;
RA   Furutani M., Iida T., Yamano S., Kamino K., Maruyama T.;
RT   "Biochemical and genetic characterization of an FK506-sensitive peptidyl
RT   prolyl cis-trans isomerase from a thermophilic archaeon, Methanococcus
RT   thermolithotrophicus.";
RL   J. Bacteriol. 180:388-394(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-11, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, AND MUTAGENESIS OF PHE-22; ASP-23 AND PHE-142.
RX   PubMed=10631007; DOI=10.1021/bi9911076;
RA   Furutani M., Ideno A., Iida T., Maruyama T.;
RT   "FK506 binding protein from a thermophilic archaeon, Methanococcus
RT   thermolithotrophicus, has chaperone-like activity in vitro.";
RL   Biochemistry 39:453-462(2000).
RN   [3] {ECO:0007744|PDB:1IX5}
RP   STRUCTURE BY NMR OF 1-151, AND DOMAIN.
RX   PubMed=12729748; DOI=10.1016/s0022-2836(03)00379-6;
RA   Suzuki R., Nagata K., Yumoto F., Kawakami M., Nemoto N., Furutani M.,
RA   Adachi K., Maruyama T., Tanokura M.;
RT   "Three-dimensional solution structure of an archaeal FKBP with a dual
RT   function of peptidyl prolyl cis-trans isomerase and chaperone-like
RT   activities.";
RL   J. Mol. Biol. 328:1149-1160(2003).
CC   -!- FUNCTION: Catalyzes the cis-trans isomerization of peptidyl prolyl
CC       bonds and accelerates protein folding (PubMed:9440528,
CC       PubMed:10631007). Also exhibits chaperone-like activity
CC       (PubMed:10631007). In vitro, can use oligopeptides such as N-succinyl-
CC       Ala-Leu-Pro-Phe-p-nitroanilide and N-succinyl-Ala-Ala-Pro-Phe-p-
CC       nitroanilide as substrates (PubMed:9440528, PubMed:10631007).
CC       {ECO:0000269|PubMed:10631007, ECO:0000269|PubMed:9440528}.
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; Evidence={ECO:0000269|PubMed:10631007,
CC         ECO:0000269|PubMed:9440528};
CC   -!- ACTIVITY REGULATION: Inhibited by FK506 but not by cyclosporine.
CC       {ECO:0000269|PubMed:10631007, ECO:0000269|PubMed:9440528}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable. {ECO:0000269|PubMed:9440528};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9440528}.
CC   -!- DOMAIN: Contains an N-terminal PPIase domain and an IF (Insert in the
CC       Flap) domain. The IF domain, formed by an insert in the flap loop, is
CC       required for the chaperone-like activity but not for the PPIase
CC       activity. {ECO:0000269|PubMed:12729748}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA24446.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; D89881; BAA24446.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_018154854.1; NZ_OX296583.1.
DR   PDB; 1IX5; NMR; -; A=1-151.
DR   PDBsum; 1IX5; -.
DR   AlphaFoldDB; O52980; -.
DR   BMRB; O52980; -.
DR   SMR; O52980; -.
DR   GeneID; 75543772; -.
DR   BRENDA; 5.2.1.8; 3266.
DR   EvolutionaryTrace; O52980; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProt.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   PANTHER; PTHR47861; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE SLYD; 1.
DR   PANTHER; PTHR47861:SF3; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE SLYD; 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; Cytoplasm; Direct protein sequencing; Isomerase;
KW   Rotamase.
FT   CHAIN           1..151
FT                   /note="Short-type peptidyl-prolyl cis-trans isomerase"
FT                   /id="PRO_0000075378"
FT   DOMAIN          8..109
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   REGION          83..132
FT                   /note="IF"
FT                   /evidence="ECO:0000305|PubMed:12729748"
FT   MUTAGEN         22
FT                   /note="F->Y: Loss of both PPIase and chaperone activities;
FT                   when associated with V-23 and Y-142."
FT                   /evidence="ECO:0000269|PubMed:10631007"
FT   MUTAGEN         23
FT                   /note="D->V: 69% of wild-type PPIase activity and 78% of
FT                   wild-type chaperone activity. Loss of both PPIase and
FT                   chaperone activities; when associated with Y-22 and Y-142."
FT                   /evidence="ECO:0000269|PubMed:10631007"
FT   MUTAGEN         142
FT                   /note="F->Y: 7% of wild-type PPIase activity and 8% of
FT                   wild-type chaperone activity. Loss of both PPIase and
FT                   chaperone activities; when associated with Y-22 and V-23."
FT                   /evidence="ECO:0000269|PubMed:10631007"
FT   STRAND          7..10
FT                   /evidence="ECO:0007829|PDB:1IX5"
FT   STRAND          23..25
FT                   /evidence="ECO:0007829|PDB:1IX5"
FT   HELIX           27..33
FT                   /evidence="ECO:0007829|PDB:1IX5"
FT   STRAND          45..48
FT                   /evidence="ECO:0007829|PDB:1IX5"
FT   TURN            49..52
FT                   /evidence="ECO:0007829|PDB:1IX5"
FT   HELIX           56..63
FT                   /evidence="ECO:0007829|PDB:1IX5"
FT   STRAND          72..75
FT                   /evidence="ECO:0007829|PDB:1IX5"
FT   TURN            77..79
FT                   /evidence="ECO:0007829|PDB:1IX5"
FT   HELIX           95..98
FT                   /evidence="ECO:0007829|PDB:1IX5"
FT   STRAND          108..114
FT                   /evidence="ECO:0007829|PDB:1IX5"
FT   STRAND          116..123
FT                   /evidence="ECO:0007829|PDB:1IX5"
FT   STRAND          126..130
FT                   /evidence="ECO:0007829|PDB:1IX5"
FT   STRAND          140..143
FT                   /evidence="ECO:0007829|PDB:1IX5"
SQ   SEQUENCE   151 AA;  16810 MW;  0F5542A74EA5386F CRC64;
     MVDKGVKIKV DYIGKLESGD VFDTSIEEVA KEAGIYAPDR EYEPLEFVVG EGQLIQGFEE
     AVLDMEVGDE KTVKIPAEKA YGNRNEMLIQ KIPRDAFKEA DFEPEEGMVI LAEGIPATIT
     EVTDNEVTLD FNHELAGKDL VFTIKIIEVV E
//