ID   A0A1G9WNH3_9ACTN        Unreviewed;       310 AA.
AC   A0A1G9WNH3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN   ORFNames=SAMN05444921_114111 {ECO:0000313|EMBL:SDM86112.1};
OS   Streptomyces wuyuanensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1196353 {ECO:0000313|EMBL:SDM86112.1, ECO:0000313|Proteomes:UP000199063};
RN   [1] {ECO:0000313|Proteomes:UP000199063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.7042 {ECO:0000313|Proteomes:UP000199063};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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, ECO:0000256|RuleBase:RU003915};
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC       {ECO:0000256|ARBA:ARBA00006577, ECO:0000256|RuleBase:RU003915}.
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DR   EMBL; FNHI01000014; SDM86112.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9WNH3; -.
DR   STRING; 1196353.SAMN05444921_114111; -.
DR   OrthoDB; 25996at2; -.
DR   Proteomes; UP000199063; Unassembled WGS sequence.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.50.40; -; 2.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   PANTHER; PTHR43811; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKPA; 1.
DR   PANTHER; PTHR43811:SF54; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKPA; 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   3: Inferred from homology;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW   ECO:0000256|RuleBase:RU003915};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199063};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW   ProRule:PRU00277}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..310
FT                   /note="Peptidyl-prolyl cis-trans isomerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011615422"
FT   DOMAIN          77..165
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   DOMAIN          224..310
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
SQ   SEQUENCE   310 AA;  32121 MW;  CFB6C53225517E03 CRC64;
     MRRLAGLLVV PLLLLSTAAC GDDKGSNSAQ TSNGLPAITA GAKFGEKPTL AKGEGEPPKD
     LKVEVISEGK GQALKKGDQA QVDYLGQVWD GDKPFDNSFD RGEPFAVTIG GGGVIEGWQK
     ALDGQKVGSR LEVSIPPSLA YGSQGQGDIP PNATLVFVMD IVKGTTLPVS AKGTEVAQDN
     IDLPKVGTNT DGKAPSITVP KKPAPTKLVS NYVIEGSGPA VKADNTVAVQ YKGVLWKDGK
     EFDSSYSKGA PVTFPLSGVI PGWSKGLEGK KVGSRVLLVV PPDMAYGDQA QGPIPAKSTL
     VFSVDILAVL
//