FKBPS_METTL
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 25-MAY-2022, entry version 85.
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 PDB; 1IX5; NMR; -; A=1-151.
DR PDBsum; 1IX5; -.
DR AlphaFoldDB; O52980; -.
DR BMRB; O52980; -.
DR SMR; O52980; -.
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 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 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
