ID E0S1U8_BUTPB Unreviewed; 315 AA.
AC E0S1U8;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN OrderedLocusNames=bpr_I1031 {ECO:0000313|EMBL:ADL33773.1};
OS Butyrivibrio proteoclasticus (strain ATCC 51982 / DSM 14932 / B316)
OS (Clostridium proteoclasticum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=515622 {ECO:0000313|EMBL:ADL33773.1, ECO:0000313|Proteomes:UP000001299};
RN [1] {ECO:0000313|EMBL:ADL33773.1, ECO:0000313|Proteomes:UP000001299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51982 / DSM 14932 / B316
RC {ECO:0000313|Proteomes:UP000001299};
RX PubMed=20689770; DOI=10.1371/journal.pone.0011942;
RA Kelly W.J., Leahy S.C., Altermann E., Yeoman C.J., Dunne J.C., Kong Z.,
RA Pacheco D.M., Li D., Noel S.J., Moon C.D., Cookson A.L., Attwood G.T.;
RT "The glycobiome of the rumen bacterium Butyrivibrio proteoclasticus B316(T)
RT highlights adaptation to a polysaccharide-rich environment.";
RL PLoS ONE 5:E11942-E11942(2010).
CC -!- FUNCTION: Also involved in hydrogenase metallocenter assembly, probably
CC by participating in the nickel insertion step. This function in
CC hydrogenase biosynthesis requires chaperone activity and the presence
CC of the metal-binding domain, but not PPIase activity.
CC {ECO:0000256|ARBA:ARBA00037071}.
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:0000256|ARBA:ARBA00000971, ECO:0000256|PROSITE-
CC ProRule:PRU00277, ECO:0000256|RuleBase:RU003915};
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC {ECO:0000256|ARBA:ARBA00006577, ECO:0000256|RuleBase:RU003915}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001810; ADL33773.1; -; Genomic_DNA.
DR RefSeq; WP_013280429.1; NC_014387.1.
DR AlphaFoldDB; E0S1U8; -.
DR STRING; 515622.bpr_I1031; -.
DR KEGG; bpb:bpr_I1031; -.
DR eggNOG; COG1047; Bacteria.
DR eggNOG; COG1433; Bacteria.
DR HOGENOM; CLU_986208_0_0_9; -.
DR Proteomes; UP000001299; Chromosome 1.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042026; P:protein refolding; IEA:UniProt.
DR CDD; cd00851; MTH1175; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 3.30.420.130; Dinitrogenase iron-molybdenum cofactor biosynthesis domain; 1.
DR InterPro; IPR003731; Di-Nase_FeMo-co_biosynth.
DR InterPro; IPR036105; DiNase_FeMo-co_biosyn_sf.
DR InterPro; IPR033913; MTH1175_dom.
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 Pfam; PF02579; Nitro_FeMo-Co; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF53146; Nitrogenase accessory factor-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW ProRule:PRU00277}; Reference proteome {ECO:0000313|Proteomes:UP000001299};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}.
FT DOMAIN 177..272
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 315 AA; 33424 MW; 0C086D2D4AACABD4 CRC64;
MKIAVTYDNG QVFQHFGHTE NFKFYEVNDN NEIVSSKVSG TNGTGHEALA DLLSDEDVDV
LICGGIGGGA MDALESNSIT VCSGASGDAD EAVKNYLSGA LESTGVNCDH HDHHHEDDAH
DEVSAQNEED IEAESGCGGC GGCGSDDEEG CGSGCGGCGG GCGGCHSGPL FEGKNVGKTC
RVHYTGTFND GTKFDSSYDR GQTLDFVCGM GMMILGFDKA VAEMNVGDII DIHLDPNEAY
GPFDPNAIIK LKISDLPGSE ELNVDERVYL QDVYGRPVPV KVIEKTDSEI TFDANHEMAG
KELNFKIELV EVKDN
//
