ID A0A1G9XD56_9ACTN Unreviewed; 230 AA.
AC A0A1G9XD56;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363019};
DE Short=PPIase {ECO:0000256|RuleBase:RU363019};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU363019};
GN ORFNames=SAMN05192576_1321 {ECO:0000313|EMBL:SDM94205.1};
OS Nocardioides szechwanensis.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1005944 {ECO:0000313|EMBL:SDM94205.1, ECO:0000313|Proteomes:UP000199004};
RN [1] {ECO:0000313|EMBL:SDM94205.1, ECO:0000313|Proteomes:UP000199004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.11147 {ECO:0000313|EMBL:SDM94205.1,
RC ECO:0000313|Proteomes:UP000199004};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. {ECO:0000256|RuleBase:RU363019}.
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|RuleBase:RU363019};
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000256|RuleBase:RU363019}.
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DR EMBL; FNIC01000001; SDM94205.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9XD56; -.
DR STRING; 1005944.SAMN05192576_1321; -.
DR OrthoDB; 5507614at2; -.
DR Proteomes; UP000199004; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR CDD; cd00317; cyclophilin; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR PANTHER; PTHR45625:SF3; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE B-RELATED; 1.
DR PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|RuleBase:RU363019, ECO:0000313|EMBL:SDM94205.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199004};
KW Rotamase {ECO:0000256|RuleBase:RU363019};
KW Signal {ECO:0000256|RuleBase:RU363019}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU363019"
FT CHAIN 23..230
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /evidence="ECO:0000256|RuleBase:RU363019"
FT /id="PRO_5039744331"
FT DOMAIN 83..229
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 21..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 230 AA; 23282 MW; EE526DC65137E7FE CRC64;
MLKRPLAAAA ALVLLAGLSA CSDDDEPTSA RDTSDQSSEQ PTNPDGADCV YEEDGAPAAK
EVDLPADQAA YDGEVAMTIS LSAGDVDVTL DAGAAPCTVN SFTSLAAQGY FDDTVCHRLT
TGPFLQVLQC GDPSASGSGG PGYSFADELT GDETYGAGTL AMANAGPDTN GSQFFIVYGD
SQLDPAYTVF GSVDPATLGV VQDIADEGVE GGYEDGPPAS PVTIEGMTVN
//