ID I4Z6V3_9BACT Unreviewed; 201 AA.
AC I4Z6V3;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=FKBP-type peptidyl-prolyl cis-trans isomerase SlyD {ECO:0000256|ARBA:ARBA00040015};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
DE AltName: Full=Metallochaperone SlyD {ECO:0000256|ARBA:ARBA00042772};
GN ORFNames=PrebiDRAFT_0151 {ECO:0000313|EMBL:EIM31945.1};
OS Prevotella bivia DSM 20514.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=868129 {ECO:0000313|EMBL:EIM31945.1, ECO:0000313|Proteomes:UP000002786};
RN [1] {ECO:0000313|EMBL:EIM31945.1, ECO:0000313|Proteomes:UP000002786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20514 {ECO:0000313|EMBL:EIM31945.1,
RC ECO:0000313|Proteomes:UP000002786};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Munk A.C.C., Kyrpides N., Mavromatis K.,
RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "Improved High-Quality Draft genome of Prevotella bivia DSM 20514.";
RL Submitted (FEB-2012) 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};
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC {ECO:0000256|ARBA:ARBA00006577}.
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; JH660660; EIM31945.1; -; Genomic_DNA.
DR RefSeq; WP_004337315.1; NZ_JH660660.1.
DR AlphaFoldDB; I4Z6V3; -.
DR GeneID; 78530214; -.
DR HOGENOM; CLU_098197_0_0_10; -.
DR Proteomes; UP000002786; Unassembled WGS sequence.
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; 2.40.10.330; -; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR048261; SlpA/SlyD-like_ins_sf.
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.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:EIM31945.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002786};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110}.
FT DOMAIN 11..77
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|Pfam:PF00254"
SQ SEQUENCE 201 AA; 22260 MW; 70B3ACA748C669C0 CRC64;
MENKNYRLII ASYELYAIEN GTETFIEKTE EDKPMSFYTD SDMVIKSFED KIRDIKDDTD
FELFLTKEEA YGEHDAKSVM VFDRSMFEQD GQLDTQSVFV GAVVPLQNEE GQRFLGKVTE
ITEDKVTVDL NHPLAGMDLK FKGHMLLNRE ADQDEVDNFF QQMNSSSSCG CGGSCGCGCS
NEGGSCNCGG NGDGNCGCGC N
//
