ID A0A2T2YC71_9BACT Unreviewed; 170 AA.
AC A0A2T2YC71;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN ORFNames=AHMF7605_06055 {ECO:0000313|EMBL:PSR53121.1};
OS Adhaeribacter arboris.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Adhaeribacter.
OX NCBI_TaxID=2072846 {ECO:0000313|EMBL:PSR53121.1, ECO:0000313|Proteomes:UP000240357};
RN [1] {ECO:0000313|EMBL:PSR53121.1, ECO:0000313|Proteomes:UP000240357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMF7605 {ECO:0000313|EMBL:PSR53121.1,
RC ECO:0000313|Proteomes:UP000240357};
RA Kang H., Kang J., Cha I., Kim H., Joh K.;
RT "Adhaeribacter sp. HMF7605 Genome sequencing and assembly.";
RL Submitted (MAR-2018) 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};
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC {ECO:0000256|ARBA:ARBA00006577}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PSR53121.1}.
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; PYFT01000001; PSR53121.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T2YC71; -.
DR OrthoDB; 9808891at2; -.
DR Proteomes; UP000240357; 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; 3.10.50.40; -; 1.
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 SUPFAM; SSF54534; FKBP-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000313|EMBL:PSR53121.1};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}.
FT DOMAIN 6..86
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 170 AA; 18582 MW; 256A6FE3589953CB CRC64;
MKISNNSVVS LTYDLSVLDE NGEKSHVETA GSDNPMVFLY GASGLPDKFE EHLNGLEEGA
TFSFSLESEE GYGDYDENAL VSIPKNVFEV DGAIPDGMLE PGNFIPMADS EGNQMQGQVV
DVNDQEVQMD FNHPLAGRTM HFDGKVVSVR EATKEELAHG HVHGEHGHHH
//
