ID A0A3M0IJY9_9ACTN Unreviewed; 334 AA.
AC A0A3M0IJY9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
GN ORFNames=CTZ28_06300 {ECO:0000313|EMBL:RMB86669.1};
OS Streptomyces shenzhenensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=943815 {ECO:0000313|EMBL:RMB86669.1, ECO:0000313|Proteomes:UP000270471};
RN [1] {ECO:0000313|EMBL:RMB86669.1, ECO:0000313|Proteomes:UP000270471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=193 {ECO:0000313|EMBL:RMB86669.1,
RC ECO:0000313|Proteomes:UP000270471};
RA Siqueira K.A., Liotti R.G., Mendes T.A.O., Soares M.A.;
RT "Draft genome of actinobacteria isolated from guarana (Paullinia cupana
RT (Mart.) Ducke.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:RMB86669.1}.
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DR EMBL; PENI01000003; RMB86669.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0IJY9; -.
DR OrthoDB; 25996at2; -.
DR Proteomes; UP000270471; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 2.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR10516; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR10516:SF464; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP12; 1.
DR Pfam; PF00254; FKBP_C; 2.
DR SUPFAM; SSF54534; FKBP-like; 2.
DR PROSITE; PS50059; FKBP_PPIASE; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW ProRule:PRU00277}; Reference proteome {ECO:0000313|Proteomes:UP000270471};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..334
FT /note="peptidylprolyl isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038829997"
FT DOMAIN 94..184
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 243..334
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REGION 23..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 334 AA; 34385 MW; 050A17BA154C170A CRC64;
MRRRSLLLAA VPAGLVTLAG CGDGKSDSSK ASASPSASGA SVSPPKIVDG PVPAITAGAK
FGEKPTVAKG SGEPSKDLAV KTVIAGGGRT VAENDFVQAH YLGQIWSSGK VFDNSYDRKS
PLVLQLAEGS VIDGWRYALT GKKAGSRIVM AVPPTWGYGS SGNAQAGIKG TDTLVFVVDV
LNTFNTKSSA QGKEVPQTDA ALPKIGTNTD GKAPSIDIPK SAAPGKLVSN YVLESDGAEV
KAEQTVLCQF QGVVWDGGKT FEQTYGSGRL SQFSLEQMKQ VVKGLSEGLT GKKVGSRVLV
VVPPDLAYGD TPPSGDVIKK GSTLVFAVDI LAAM
//
