ID A0A101CPT0_9FLAO Unreviewed; 229 AA.
AC A0A101CPT0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN ORFNames=AR687_19810 {ECO:0000313|EMBL:KUJ60147.1};
OS Flavobacteriaceae bacterium CRH.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1742859 {ECO:0000313|EMBL:KUJ60147.1, ECO:0000313|Proteomes:UP000053826};
RN [1] {ECO:0000313|EMBL:KUJ60147.1, ECO:0000313|Proteomes:UP000053826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRH {ECO:0000313|EMBL:KUJ60147.1,
RC ECO:0000313|Proteomes:UP000053826};
RA Newman J.D., Miller J.R., Jacobs K.T.;
RT "Genome Sequence of Flavobacterium sp. CHR.";
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, ECO:0000256|RuleBase:RU003915};
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC {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:KUJ60147.1}.
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DR EMBL; LMAJ01000023; KUJ60147.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101CPT0; -.
DR STRING; 1742859.AR687_19810; -.
DR OrthoDB; 1093155at2; -.
DR Proteomes; UP000053826; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR019869; Motility-assoc_PPIase_GldI.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR NCBIfam; TIGR03516; ppisom_GldI; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000256|RuleBase:RU003915};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}.
FT DOMAIN 93..180
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REGION 188..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 229 AA; 25786 MW; 23DAE36FE53654AB CRC64;
MNYLKRSIYT LLFAVLLVGC KQHEDVRRPI SRSSGSFMKK SADRNKKLVA NEEDVIKKII
KSNPKVKYYA TRKGYWFSYD EQNTTETQTP RKGDIAYFNL EIKNIKGQVI YSESELGPQT
YYVDKQDIMM GLRDGIKLMH KNETVTFLFP SHIAYGYHGD NKKIGTNESL MCTVTLRNFV
PDPASVKTAA TAPATTSPTT TVAKTTTAQN PKPAAPKTVS QTKKDTLKP
//
