ID D4LVJ8_9FIRM Unreviewed; 283 AA.
AC D4LVJ8;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN ORFNames=CK5_36550 {ECO:0000313|EMBL:CBL24806.1};
OS Blautia obeum A2-162.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=657314 {ECO:0000313|EMBL:CBL24806.1, ECO:0000313|Proteomes:UP000008955};
RN [1] {ECO:0000313|EMBL:CBL24806.1, ECO:0000313|Proteomes:UP000008955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A2-162 {ECO:0000313|EMBL:CBL24806.1,
RC ECO:0000313|Proteomes:UP000008955};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Ruminococcus obeum A2-162.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL24806.1, ECO:0000313|Proteomes:UP000008955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A2-162 {ECO:0000313|EMBL:CBL24806.1,
RC ECO:0000313|Proteomes:UP000008955};
RA Pajon A.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FP929054; CBL24806.1; -; Genomic_DNA.
DR AlphaFoldDB; D4LVJ8; -.
DR KEGG; rob:CK5_36550; -.
DR PATRIC; fig|657314.3.peg.3528; -.
DR HOGENOM; CLU_986208_0_0_9; -.
DR Proteomes; UP000008955; Chromosome.
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};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}.
FT DOMAIN 147..232
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 283 AA; 29914 MW; 547CDE66837374B8 CRC64;
MKIAVTYDNG NVFQHFGKTE NFKVYEVEDD KVVSSEVIGS NGTGHGALAG LLAEQGINVL
ICGGIGGGAQ AALTEAGIEM VAGAQGNTDD VVKAYLKGEL VSTGANCDHH HHEEGHSCGS
HEEGHSCGGS CGGCGGHKSD ITGPNVGKTC RTHYKGTFND GTQFDSSYDR GEPLEFICGA
GQMIKGFDAA VANMEIGEIK EVHLMPEEAY GQANPDAIFT LEIAQLPGSE NLEVGQQVYL
SNQYGQPFPV KVTAKEETTI TFDANHEMAG KELNFTIELV EVK
//
