ID A0A371IK95_9FIRM Unreviewed; 384 AA.
AC A0A371IK95;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN ORFNames=BBG48_007590 {ECO:0000313|EMBL:RDY20917.1};
OS Criibacterium bergeronii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Criibacterium.
OX NCBI_TaxID=1871336 {ECO:0000313|EMBL:RDY20917.1, ECO:0000313|Proteomes:UP000093352};
RN [1] {ECO:0000313|EMBL:RDY20917.1, ECO:0000313|Proteomes:UP000093352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCRI-22567 {ECO:0000313|EMBL:RDY20917.1,
RC ECO:0000313|Proteomes:UP000093352};
RX PubMed=27587833;
RA Maheux A.F., Berube E., Boudreau D.K., Raymond F., Corbeil J., Roy P.H.,
RA Boissinot M., Omar R.F.;
RT "Draft Genome Sequence of Criibacterium bergeronii gen. nov., sp. nov.,
RT Strain CCRI-22567T, Isolated from a Vaginal Sample from a Woman with
RT Bacterial Vaginosis.";
RL Genome Announc. 4:e00959-16(2016).
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};
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:RDY20917.1}.
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DR EMBL; MBEW02000017; RDY20917.1; -; Genomic_DNA.
DR RefSeq; WP_068913208.1; NZ_MBEW02000017.1.
DR AlphaFoldDB; A0A371IK95; -.
DR STRING; 1871336.BBG48_09845; -.
DR Proteomes; UP000093352; 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:UP000093352};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..384
FT /note="peptidylprolyl isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016868756"
FT DOMAIN 179..284
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 335..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 384 AA; 43306 MW; 90A68A58635FD7D5 CRC64;
MKRILKSALA VLLALTVAAC GSKSGKAIAT VNGENITYSR YVQELALFKS QIQMQFGDSI
WSQTFPGSDE TFLQNLKTQI LDNLVVNTLL KQEAEKAGLK LDEAKYNEAV KQTLDGMNKD
EMLKKYYEDN KINEEYIKQM IKESMLAQAY HDDYISKNAA TEDEIKKYYE DNKATQFTDE
QVKASHILIK TQDQDGNPLP QDQQDAAKAK IDDIAKKIKA GESFEALAKE FSQDGSKDNG
GDLGYFRKNE MVPEFEQKAF SMNVGEISEP VKTQYGYHLI KLTDKKSSTP TLEEVKDSIK
STIEEKKFSD YLTKLKDDKE KVKKSEDLLK DAEKDIKEDA LKQEPAADKN ATKDETSKEQ
TKDAAKDAPA TEQKETDKTE SKAK
//
