ID A0A0A2FJ74_9PORP Unreviewed; 194 AA.
AC A0A0A2FJ74;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN ORFNames=HQ45_05005 {ECO:0000313|EMBL:KGN90162.1};
OS Porphyromonas crevioricanis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=393921 {ECO:0000313|EMBL:KGN90162.1, ECO:0000313|Proteomes:UP000030139};
RN [1] {ECO:0000313|EMBL:KGN90162.1, ECO:0000313|Proteomes:UP000030139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-253 OH2125 {ECO:0000313|Proteomes:UP000030139};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT "Porphyromonas crevioricanis strain:COT-253_OH2125 Genome sequencing.";
RL Submitted (AUG-2014) 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, ECO:0000256|PROSITE-
CC ProRule:PRU00277, ECO:0000256|RuleBase:RU003915};
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC {ECO:0000256|ARBA:ARBA00006577, ECO:0000256|RuleBase:RU003915}.
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:KGN90162.1}.
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; JQJB01000006; KGN90162.1; -; Genomic_DNA.
DR RefSeq; WP_023936950.1; NZ_LS483447.1.
DR AlphaFoldDB; A0A0A2FJ74; -.
DR STRING; 393921.HQ45_05005; -.
DR eggNOG; COG0545; Bacteria.
DR OrthoDB; 9814548at2; -.
DR Proteomes; UP000030139; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 1.10.287.460; Peptidyl-prolyl cis-trans isomerase, FKBP-type, N-terminal domain; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR000774; PPIase_FKBP_N.
DR InterPro; IPR036944; PPIase_FKBP_N_sf.
DR PANTHER; PTHR43811:SF23; FKBP-TYPE 22 KDA PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR PANTHER; PTHR43811; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKPA; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF01346; FKBP_N; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000256|RuleBase:RU003915};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}.
FT DOMAIN 108..194
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 194 AA; 21387 MW; C9212714ABADDFE6 CRC64;
MDKISYALGL SIANNFRATG IETVDMDEFV RAMNDVMHGK QTAITYEEAQ QVLNSFFAAL
QERVKDQNKE AGKEFLKING MKRGVTTTET GLQYEILVKG DGPKPKLEDT VRCHYHGTLI
NGEVFDSSKQ RGEPAEFPLK GVISGWTEVL QLMPVGSTWR VTIPSELAYG ERGAGSSIGP
NSTLIFDIEL QAIV
//
