ID A0A0X3XQ64_9ACTN Unreviewed; 333 AA.
AC A0A0X3XQ64;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
GN ORFNames=ADL34_17085 {ECO:0000313|EMBL:KUL74432.1};
OS Streptomyces sp. NRRL WC-3605.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609103 {ECO:0000313|EMBL:KUL74432.1, ECO:0000313|Proteomes:UP000052945};
RN [1] {ECO:0000313|EMBL:KUL74432.1, ECO:0000313|Proteomes:UP000052945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3605 {ECO:0000313|EMBL:KUL74432.1,
RC ECO:0000313|Proteomes:UP000052945};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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};
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:KUL74432.1}.
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DR EMBL; LLZN01000056; KUL74432.1; -; Genomic_DNA.
DR RefSeq; WP_062672155.1; NZ_LLZN01000056.1.
DR AlphaFoldDB; A0A0X3XQ64; -.
DR OrthoDB; 25996at2; -.
DR Proteomes; UP000052945; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR Gene3D; 3.10.50.40; -; 2.
DR InterPro; IPR044609; FKBP2/11.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR45779; PEPTIDYLPROLYL ISOMERASE; 1.
DR PANTHER; PTHR45779:SF6; PEPTIDYLPROLYL ISOMERASE; 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 4: Predicted;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000313|EMBL:KUL74432.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000052945};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}.
FT DOMAIN 96..186
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 245..333
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REGION 20..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 333 AA; 34983 MW; 0420E91991876EE2 CRC64;
MRRRSLLIAV PAGMVTLAAC GDDKDSGGEA SDSVSPSAPE QSAAPSPKIV DGPLPAITAG
TKFGEKPTVA KGEGEPSKDL AVRTVVAGNG KTVAENDYLQ ANYLGQIWAT AKVFDNSYDR
KTPLLIQLSQ GRIIDGWRYA LTGKKVGSRV EMAVPPTWGY GKEGNEQAGI KGTDTLVFVV
DIEDSFNASS SAKGTKVAQD DADLPKVGTN TDGKAPSIEV PKTDPPKKLV SNYILEGDGD
EVAAENTVLV QYKGVQWDTG KEFDSSYAAK QLVSFPLAQV VKGWSQGLAG KKVGSRVLIA
IPPELGYGDQ PPQGSGIAKN ATLVFSVDIL AKM
//
