ID A0A6G2W2Y9_9ACTN Unreviewed; 176 AA.
AC A0A6G2W2Y9;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 08-NOV-2023, entry version 11.
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=GT346_40265 {ECO:0000313|EMBL:MYW49372.1};
OS Streptomyces sp. SID161.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2690251 {ECO:0000313|EMBL:MYW49372.1, ECO:0000313|Proteomes:UP000479902};
RN [1] {ECO:0000313|EMBL:MYW49372.1, ECO:0000313|Proteomes:UP000479902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SID161 {ECO:0000313|EMBL:MYW49372.1,
RC ECO:0000313|Proteomes:UP000479902};
RX PubMed=30705269; DOI=.1038/s41467-019-08438-0;
RA Chevrette M.G., Carlson C.M., Ortega H.E., Thomas C., Ananiev G.E.,
RA Barns K.J., Book A.J., Cagnazzo J., Carlos C., Flanigan W., Grubbs K.J.,
RA Horn H.A., Hoffmann F.M., Klassen J.L., Knack J.J., Lewin G.R.,
RA McDonald B.R., Muller L., Melo W.G.P., Pinto-Tomas A.A., Schmitz A.,
RA Wendt-Pienkowski E., Wildman S., Zhao M., Zhang F., Bugni T.S., Andes D.R.,
RA Pupo M.T., Currie C.R.;
RT "The antimicrobial potential of Streptomyces from insect microbiomes.";
RL Nat. Commun. 10:516-516(2019).
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|ARBA:ARBA00002388,
CC 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|ARBA:ARBA00007365, ECO:0000256|RuleBase:RU363019}.
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:MYW49372.1}.
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DR EMBL; WWKG01001802; MYW49372.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6G2W2Y9; -.
DR Proteomes; UP000479902; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
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 PIRSF; PIRSF001467; Peptidylpro_ismrse; 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:MYW49372.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000479902};
KW Rotamase {ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 11..171
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 176 AA; 19117 MW; 95B6DA80917A6C7C CRC64;
MAEQLYATLR TSLGEIEVRL FPQHAPVTVR NFVELARGER EWTHPGTGVR SRDRLYDGTV
FHSVIDGFMI QGGDPLGNGL GGPGYGFEDE CHPDLAFDTP YLMAMANAGP GTNGSQFFIT
VTPSTWLNGK RTIFGEVSGP AGRKVVDAIA RVPTGRNDRP LADVVLETVV VRTREG
//
