ID A0A2U2PAL2_9SPHI Unreviewed; 292 AA.
AC A0A2U2PAL2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN ORFNames=DDR33_22460 {ECO:0000313|EMBL:PWG78441.1};
OS Pararcticibacter amylolyticus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pararcticibacter.
OX NCBI_TaxID=2173175 {ECO:0000313|EMBL:PWG78441.1, ECO:0000313|Proteomes:UP000245647};
RN [1] {ECO:0000313|EMBL:PWG78441.1, ECO:0000313|Proteomes:UP000245647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJ4-8 {ECO:0000313|EMBL:PWG78441.1,
RC ECO:0000313|Proteomes:UP000245647};
RA Cai Y.;
RT "Pedobacter chongqingensis sp. nov., isolated from a rottenly hemp rope.";
RL Submitted (APR-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}.
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:PWG78441.1}.
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DR EMBL; QEAS01000025; PWG78441.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2PAL2; -.
DR OrthoDB; 669809at2; -.
DR Proteomes; UP000245647; 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: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.
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:UP000245647};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}.
FT DOMAIN 66..163
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 208..291
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 292 AA; 32436 MW; 1FE6F7B668574483 CRC64;
MRTMTYKVYF FVLLLAAVIT GCEKSYESIE TEDEKNIQAY IQKNGLNVTQ YDTTGIYYQI
TSTPPEQADS LDYTKQLPII YTVRSLDGAY SSQDTVLNRY GNYFGYFSPA GIRDIVKRAL
KKQGGEIRII VPSRKAYGRS GNKTLGIPGN ASLDYTIKVL ESKKLPQYED GMIRKYLERE
GLTGFTRTES GLFYKILEQG TGSSITIDST VTTDYTGKLL NGQVFDSRTS SVFSLTDPGL
RQGWKEALPL LKEGGSIRMV FPSPLGYGIT GYSGIPAFSP LDFEVKVTAV SN
//
