ID   A0A2X4WV50_9NOCA        Unreviewed;       240 AA.
AC   A0A2X4WV50;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN   Name=fkbP {ECO:0000313|EMBL:SQI30885.1};
GN   ORFNames=NCTC10994_01795 {ECO:0000313|EMBL:SQI30885.1};
OS   Rhodococcus coprophilus.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=38310 {ECO:0000313|EMBL:SQI30885.1, ECO:0000313|Proteomes:UP000249091};
RN   [1] {ECO:0000313|EMBL:SQI30885.1, ECO:0000313|Proteomes:UP000249091}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC10994 {ECO:0000313|EMBL:SQI30885.1,
RC   ECO:0000313|Proteomes:UP000249091};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) 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; LS483468; SQI30885.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2X4WV50; -.
DR   STRING; 1219011.GCA_001895045_02888; -.
DR   KEGG; rcr:NCTC10994_01795; -.
DR   Proteomes; UP000249091; Chromosome 1.
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:SF19; 39 KDA FK506-BINDING NUCLEAR PROTEIN; 1.
DR   PANTHER; PTHR43811; 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.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW   ECO:0000256|RuleBase:RU003915};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249091};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW   ProRule:PRU00277}.
FT   DOMAIN          33..119
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   DOMAIN          154..240
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
SQ   SEQUENCE   240 AA;  25571 MW;  D093668D50658169 CRC64;
     MSKPEIEFQE GPAPTELVIK DITIGDGPEA TPGAVVDVHY VGVEFDTGEE FDSSWSRGES
     IRFPLSGLIA GWQEGIPGMR VGGRRQLTIP PELAYGPAGS GHQLSGKTLV FVIDLLDVQV
     QPEPPVIEKS EGPAPTELVV EDITIGEGPE AQPDATVDVH YKGVEYETNE EFDSSWSRGQ
     SVAFPLGRLI PGWQQGIPGM RVGGRRKLTV PPELAYGPAG SGHPLGGKTL VFVIDLVGLP
//