ID A0A068YRT7_9BURK Unreviewed; 174 AA.
AC A0A068YRT7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
OS Polaromonas sp. CG9_12.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1504672 {ECO:0000313|EMBL:CDS54075.1, ECO:0000313|Proteomes:UP000043372};
RN [1] {ECO:0000313|EMBL:CDS54075.1, ECO:0000313|Proteomes:UP000043372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Smith H.J., Foreman C.M., Ramaraj T.;
RT "Draft Genome Sequence of a Metabolically Diverse Antarctic Supraglacial
RT Stream Organism, Polaromonas sp. Strain CG9_12, Determined Using Pacific
RT Biosciences Single-Molecule Real-Time Sequencing Technology.";
RL Genome Announc. 2:1-2(2014).
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}.
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DR EMBL; CCJP01000005; CDS54075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068YRT7; -.
DR STRING; 1504672.gene:199033323; -.
DR eggNOG; COG1047; Bacteria.
DR OrthoDB; 9808891at2; -.
DR Proteomes; UP000043372; 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:CDS54075.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000043372};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}.
FT DOMAIN 4..87
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 174 AA; 18728 MW; EE9B1FEB35FF1F28 CRC64;
MKITPQCVVA LTWTLKDTLG DVLDELDEPV DFLLGGKDLL ASIEEALLGH AAGDTLELHL
EPENAFGDYD ENRVFLEPRS IFPAELEEGM TFDGAAMPAG ATAKIPPEHI YTVTDIYPEH
VVLDGNHPLG GIAIRLALKV ESVREATESE IGQGSLGTGF FKLESTATGN DTLH
//
