FKBPL_METTH
ID FKBPL_METTH Reviewed; 250 AA.
AC O27197;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, 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:0000269|PubMed:10824098};
DE AltName: Full=FKBP-type peptidyl-prolyl cis-trans isomerase {ECO:0000305};
DE Short=FKBP-type PPIase {ECO:0000305};
DE AltName: Full=Long type FKBP {ECO:0000303|PubMed:10824098};
DE AltName: Full=MbFK {ECO:0000303|PubMed:10824098};
DE AltName: Full=Rotamase {ECO:0000305};
GN OrderedLocusNames=MTH_1125 {ECO:0000312|EMBL:AAB85614.1};
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND DOMAIN.
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=10824098; DOI=10.1046/j.1432-1327.2000.01332.x;
RA Ideno A., Yoshida T., Furutani M., Maruyama T.;
RT "The 28.3 kDa FK506 binding protein from a thermophilic archaeum,
RT Methanobacterium thermoautotrophicum, protects the denaturation of proteins
RT in vitro.";
RL Eur. J. Biochem. 267:3139-3149(2000).
CC -!- FUNCTION: Catalyzes the cis-trans isomerization of peptidyl prolyl
CC bonds and accelerates protein folding. Also exhibits chaperone-like
CC activity (PubMed:10824098). In vitro, can use oligopeptides such as N-
CC succinyl-Ala-Leu-Pro-Phe-p-nitroanilide and N-succinyl-Ala-Ala-Pro-Phe-
CC p-nitroanilide as substrates. The PPIase activity is much lower than
CC those of other FKBPs reported against oligopeptidyl substrates. As a
CC chaperone, protects green fluorescent protein (GFP) and rhodanese from
CC thermal denaturation or aggregation, and suppresses the aggregation of
CC chemically unfolded rhodanese and elevates the yield of its refolding
CC (PubMed:10824098). {ECO:0000269|PubMed:10824098}.
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:0000269|PubMed:10824098};
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:10824098}.
CC -!- DOMAIN: Contains an N-terminal PPIase domain, an IF (Insert in the
CC Flap) domain and a C-terminal domain (CTD). Aggregation suppressing
CC activity against chemically unfolded protein is exerted mainly by the
CC CTD while N- and C-terminal domains contribute to thermal protein
CC aggregation suppression. The CTD probably contributes to
CC hexamerization. {ECO:0000269|PubMed:10824098}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR EMBL; AE000666; AAB85614.1; -; Genomic_DNA.
DR PIR; G69016; G69016.
DR RefSeq; WP_010876749.1; NC_000916.1.
DR AlphaFoldDB; O27197; -.
DR SMR; O27197; -.
DR STRING; 187420.MTH_1125; -.
DR EnsemblBacteria; AAB85614; AAB85614; MTH_1125.
DR GeneID; 1471533; -.
DR KEGG; mth:MTH_1125; -.
DR PATRIC; fig|187420.15.peg.1102; -.
DR HOGENOM; CLU_073526_0_0_2; -.
DR OMA; IREFHRH; -.
DR Proteomes; UP000005223; 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 Chaperone; Isomerase; Reference proteome; Rotamase.
FT CHAIN 1..250
FT /note="Long-type peptidyl-prolyl cis-trans isomerase"
FT /id="PRO_0000449237"
FT DOMAIN 6..94
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REGION 85..136
FT /note="IF"
FT /evidence="ECO:0000250|UniProtKB:Q58235"
FT REGION 157..250
FT /note="CTD"
FT /evidence="ECO:0000305|PubMed:10824098"
SQ SEQUENCE 250 AA; 28318 MW; E30B9084E3D00718 CRC64;
MAVNKGDFIK IEFTGKVKET GEVFDTTYEE VAREAGLGIK KIFGPIPVVV GGGHLIKGLD
EAVIGMEEGE EKHVEIEPED AFGNRDPKLV QLIPMGEFKR QGIKPYPGMT LTVEGHEGRV
LNVSGGRVRV DFNHELAGKT LEYDLKVKEI ITDDAEKVKS MIQLHYPSQN MDIDKTEVKI
EDGKVIIHMD EMTRFDNRSY MDVTLARFRI ARDIWENIEG VEKVEFADVF EKRDMEAEEK
EEEVEDAGED
