ID A0A516RHQ3_STRST Unreviewed; 163 AA.
AC A0A516RHQ3;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=FH965_35295 {ECO:0000313|EMBL:QDQ15175.1};
OS Streptomyces spectabilis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68270 {ECO:0000313|EMBL:QDQ15175.1, ECO:0000313|Proteomes:UP000316806};
RN [1] {ECO:0000313|EMBL:QDQ15175.1, ECO:0000313|Proteomes:UP000316806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 2792 {ECO:0000313|EMBL:QDQ15175.1,
RC ECO:0000313|Proteomes:UP000316806};
RX PubMed=31197515;
RA Sinha A., Phillips-Salemka S., Niraula T.A., Short K.A., Niraula N.P.;
RT "The complete genomic sequence of Streptomyces spectabilis NRRL-2792 and
RT identification of secondary metabolite biosynthetic gene clusters.";
RL J. Ind. Microbiol. Biotechnol. 46:1217-1223(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|ARBA:ARBA00000971,
CC ECO:0000256|RuleBase:RU363019};
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000256|ARBA:ARBA00007365, ECO:0000256|RuleBase:RU363019}.
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DR EMBL; CP040916; QDQ15175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A516RHQ3; -.
DR Proteomes; UP000316806; Chromosome.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE H; 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; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU363019};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 5..161
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 163 AA; 17541 MW; 620987C352A9D2DB CRC64;
MQNVYFDITI DGKDAGRIVF RLFDDVVPET ARNFRELATG QNGYGYAGSA FHRVIPQFML
QGGDFTHGNG TGGKSIFGAT FADENFSLKH DRPFLLSMAN RGPNTNSSQF FVTTVVTPWL
DGKHVVFGEV AEGEDLVKQI EALGSGSGAL ASDVVIKESG TVA
//
