ID A0A2S0UDI3_9BACL Unreviewed; 405 AA.
AC A0A2S0UDI3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN ORFNames=DCC85_17420 {ECO:0000313|EMBL:AWB45790.1};
OS Paenibacillus sp. CAA11.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1532905 {ECO:0000313|EMBL:AWB45790.1, ECO:0000313|Proteomes:UP000244407};
RN [1] {ECO:0000313|EMBL:AWB45790.1, ECO:0000313|Proteomes:UP000244407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAA11 {ECO:0000313|EMBL:AWB45790.1,
RC ECO:0000313|Proteomes:UP000244407};
RA Um Y., Kim S., Gong G.;
RT "Complete genome of CAA11.";
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};
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DR EMBL; CP028922; AWB45790.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0UDI3; -.
DR OrthoDB; 14196at2; -.
DR Proteomes; UP000244407; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 1.10.4030.10; Porin chaperone SurA, peptide-binding domain; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR023058; PPIase_PpiC_CS.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR PANTHER; PTHR47245:SF1; FOLDASE PROTEIN PRSA; 1.
DR PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR Pfam; PF13145; Rotamase_2; 1.
DR Pfam; PF13624; SurA_N_3; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW ProRule:PRU00278}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000244407};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 104..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 255..345
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 405 AA; 44000 MW; 9AA4107015CCC30A CRC64;
MTEEKKDPQD TQPEAAEPLN ESQSETTETT KNTENTDTSS AVNEPATGSG QEAPKSETEE
VGQTEENTSV LVPEGEALAS ISATEGTDHP AAEEESTKRG GSQVWIGISL LLAVLLVISL
VKNPFGQSDA KTVVATVNGE DITKDKLYDK LVEAGGTQTL SGMIDEELVR QEMEKEKLQI
TDADIKKEKD FYLKQFGSDE ALSQVLAQYG MSEEDFNEQL KKEAQIRKLL EPKVTVTDDE
IKQYFEANKE AMNTPEQAKF SSILVATQPE AEAIIKELKG GADFAKLAKE KSIDTTTKDK
GGDLGYVSKG TQDAAFDEAA FKLKKGEISG AIKSDAGFQV LKMTDYKQAH TATLEEKKAE
IKDMIVTQKV SEKATTWLAD LKSKAKITNT LENKANEKAA AAPAK
//
