ID A0A1W1XE30_9NEIS Unreviewed; 241 AA.
AC A0A1W1XE30;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-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=SAMN02745857_01235 {ECO:0000313|EMBL:SMC21761.1};
OS Andreprevotia lacus DSM 23236.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chitinibacteraceae; Andreprevotia.
OX NCBI_TaxID=1121001 {ECO:0000313|EMBL:SMC21761.1, ECO:0000313|Proteomes:UP000192761};
RN [1] {ECO:0000313|EMBL:SMC21761.1, ECO:0000313|Proteomes:UP000192761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23236 {ECO:0000313|EMBL:SMC21761.1,
RC ECO:0000313|Proteomes:UP000192761};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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};
CC -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC {ECO:0000256|ARBA:ARBA00007656}.
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DR EMBL; FWXD01000006; SMC21761.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1XE30; -.
DR STRING; 1121001.SAMN02745857_01235; -.
DR OrthoDB; 9769613at2; -.
DR Proteomes; UP000192761; 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 InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR PANTHER; PTHR47245:SF2; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE HP_0175-RELATED; 1.
DR PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR Pfam; PF00639; Rotamase; 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:SMC21761.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000192761};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278}.
FT DOMAIN 92..192
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 241 AA; 25889 MW; A3446E13FD6CD13A CRC64;
MTITVNGVEI SQARIDAEVP NFEGAPSPID AATQQLILHE LLLQTAVAQG LTGETEDEKI
GALLDTAIQV APAGEAECRA FYEQNPQSFV RGEQVEASHI LFSAENGVPA SLVRAKAEGI
LAELKAEPYK FEAYAREHSA CPSGKQGGNL GNFGRGQMVP EFDAAAFALN EGELSPELVE
TQFGFHIIKA GKKTAGESVS FDEVQEQLQD YLTKMAGRRA MNEYLGTLVK GAKIEGYQLE
A
//