ID A0A1I2BC06_9FIRM Unreviewed; 365 AA.
AC A0A1I2BC06;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN ORFNames=SAMN02910278_01058 {ECO:0000313|EMBL:SFE53418.1};
OS Peptostreptococcus sp. D1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptostreptococcus.
OX NCBI_TaxID=72304 {ECO:0000313|EMBL:SFE53418.1, ECO:0000313|Proteomes:UP000199190};
RN [1] {ECO:0000313|EMBL:SFE53418.1, ECO:0000313|Proteomes:UP000199190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1 {ECO:0000313|EMBL:SFE53418.1,
RC ECO:0000313|Proteomes:UP000199190};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FONP01000005; SFE53418.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2BC06; -.
DR STRING; 72304.SAMN02910278_01058; -.
DR OrthoDB; 14196at2; -.
DR Proteomes; UP000199190; Unassembled WGS sequence.
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; PF13616; Rotamase_3; 1.
DR Pfam; PF13623; SurA_N_2; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW ProRule:PRU00278}; Reference proteome {ECO:0000313|Proteomes:UP000199190};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..365
FT /note="peptidylprolyl isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038686109"
FT DOMAIN 170..276
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 328..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 365 AA; 40798 MW; 9D8D27EE74E48AF0 CRC64;
MKKLLSVVTA VAIGFVSVAC SSTKDAVALV DGKPIAKQEF EENLKFNKWA MEQQYGDKVW
EQVEKQNPDF QNSIKANVLN QMVQSRIVLN YAEKNNIKAD EAQLKQFNDN LKKTLADKTK
KASFDKDGLT EEALKKYGEQ AAIMTAFSKY VAKKAEPTET ELNEYYEKNK EKVDASHILL
STTDASGKPM TEEKKAEVKK KADELYSQLK NGADFAKLAK ENSADPGSAQ NGGSLGEFGK
GKMVKEFEEV AFSLKEGEIS KPVASQYGYH IIKVNKKVTS KYNDVKNELK SELTQTRTQE
LIKKIQESST VEKYEDKIKD IKFVEVKKST TTDDKSTTDS KSTDSKSTDS KSTDSKATEK
KSEDK
//
