ID A0A1P8S0C9_9FLAO Unreviewed; 235 AA.
AC A0A1P8S0C9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=BWZ20_13630 {ECO:0000313|EMBL:APY09277.1};
OS Winogradskyella sp. J14-2.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=1936080 {ECO:0000313|EMBL:APY09277.1, ECO:0000313|Proteomes:UP000187462};
RN [1] {ECO:0000313|EMBL:APY09277.1, ECO:0000313|Proteomes:UP000187462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J14-2 {ECO:0000313|EMBL:APY09277.1,
RC ECO:0000313|Proteomes:UP000187462};
RA Kim J.H., Chi W.-J.;
RT "Genome sequence of Winogradskyella sp. J14-2 isolated from seawater in
RT Jeju island.";
RL Submitted (JAN-2017) 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; CP019388; APY09277.1; -; Genomic_DNA.
DR RefSeq; WP_076620736.1; NZ_CP019388.1.
DR AlphaFoldDB; A0A1P8S0C9; -.
DR STRING; 1936080.BWZ20_13630; -.
DR KEGG; wij:BWZ20_13630; -.
DR OrthoDB; 9807797at2; -.
DR Proteomes; UP000187462; Chromosome.
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; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR PANTHER; PTHR45625:SF4; PEPTIDYLPROLYL ISOMERASE DOMAIN AND WD REPEAT-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|RuleBase:RU363019, ECO:0000313|EMBL:APY09277.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000187462};
KW Rotamase {ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 83..233
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 235 AA; 27455 MW; 61A2700A848DACB4 CRC64;
MRFQLLFIIV LFLWNCEDKQ TSKNSNTTVV KDTITTKAKP ITKKKAKKSS EFPVLTDANA
MEFFLEYDKE HKENKVRVTT DFGSFDILLY DKTKFHRSNF IYLTKRKYFN GTQFYRVIKD
FVVQGGSSDA LDLYKKRRKI GHYLLPPDTK RGYTHQRGSV SMPSSEIENA YKLASPFQFF
IVINRERAKH LDGDYTVFGE VIRGMDVVDK INAVKTDEGD WPLKNVYIKK VEIIE
//
