ID A0A229FSW3_9BURK Unreviewed; 268 AA.
AC A0A229FSW3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Peptidylprolyl isomerase {ECO:0000313|EMBL:OXL14658.1};
GN ORFNames=AOC33_09005 {ECO:0000313|EMBL:OXL14658.1};
OS Polynucleobacter cosmopolitanus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=351345 {ECO:0000313|EMBL:OXL14658.1, ECO:0000313|Proteomes:UP000215188};
RN [1] {ECO:0000313|EMBL:OXL14658.1, ECO:0000313|Proteomes:UP000215188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWH-MoIso2 {ECO:0000313|EMBL:OXL14658.1,
RC ECO:0000313|Proteomes:UP000215188};
RA Hahn M.W.;
RT "Reclassification of a Polynucleobacter cosmopolitanus strain isolated from
RT tropical Lake Victoria as Polynucleobacter victoriensis comb. nov.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC {ECO:0000256|ARBA:ARBA00007656}.
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:OXL14658.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NJGG01000003; OXL14658.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A229FSW3; -.
DR OrthoDB; 14196at2; -.
DR Proteomes; UP000215188; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.1040; -; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
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 SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:OXL14658.1};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..268
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012104466"
FT DOMAIN 132..223
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 268 AA; 29581 MW; 246C55A5A353D762 CRC64;
MKKLLPTLAL SVAATMTITG ALSTPALAQN AAVVNGKAIP KAKLDKLIAN SGQGSNPELR
ERARDMLITR ELINQEAIKR GLLTNDDIQE QLEQARLNIL VGAVFEDYIA RGGVSDAELK
ASYEQIKTQF EGTEYKVRHI LVEKEADAKA LIAKIKAGEK FEDLAKANSK DPGSAANGGD
LDWMTPQALV PEFSKVMVAL QKGQMTEKPV KSQFGFHVIR VDDMRQAKVP DLAELKPQLI
QMMSQDQNWQ RAKFEEMLKN LKAKAKIQ
//
