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Database: UniProt
Entry: A0A238WI82_9FLAO
LinkDB: A0A238WI82_9FLAO
Original site: A0A238WI82_9FLAO 
ID   A0A238WI82_9FLAO        Unreviewed;       276 AA.
AC   A0A238WI82;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN   ORFNames=SAMN06265371_103248 {ECO:0000313|EMBL:SNR46272.1};
OS   Lutibacter agarilyticus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Lutibacter.
OX   NCBI_TaxID=1109740 {ECO:0000313|EMBL:SNR46272.1, ECO:0000313|Proteomes:UP000198384};
RN   [1] {ECO:0000313|EMBL:SNR46272.1, ECO:0000313|Proteomes:UP000198384}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29150 {ECO:0000313|EMBL:SNR46272.1,
RC   ECO:0000313|Proteomes:UP000198384};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-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, ECO:0000256|PROSITE-
CC         ProRule:PRU00277, ECO:0000256|RuleBase:RU003915};
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC       {ECO:0000256|RuleBase:RU003915}.
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DR   EMBL; FZNT01000003; SNR46272.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238WI82; -.
DR   Proteomes; UP000198384; Unassembled WGS sequence.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.50.40; -; 2.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   PANTHER; PTHR10516; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR10516:SF464; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKBP12; 1.
DR   Pfam; PF00254; FKBP_C; 2.
DR   SUPFAM; SSF54534; FKBP-like; 2.
DR   PROSITE; PS50059; FKBP_PPIASE; 2.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW   ProRule:PRU00277}; Reference proteome {ECO:0000313|Proteomes:UP000198384};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW   ProRule:PRU00277}.
FT   DOMAIN          66..150
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
FT   DOMAIN          192..275
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
SQ   SEQUENCE   276 AA;  29991 MW;  991CB4C31202BF4F CRC64;
     MKYFISLLLL VSFISCNKDE ENEYLGQTED DIIQYIEDNN LDATRTKNGV YYVIDEEGEG
     SFPFEDAYVT VKYTGYFLDG KEFDASGTNG AMFDLLAVIP GFSEGIVNFN NGSSGTMFIP
     PSLGYGASGV NGFIPGGAVL IFDVEVVKIT NPQTEVDIID YLETNNLEAE RSDTGLYYII
     EEPGTGDPIT ESSIVTVAYT GYFLDGVEFD ASSNSGVQFS LQNLISGFKE GLTYFKEGGK
     GTLLLPPELA YGDEGSATVP RSAVLIFEVD VKSLDN
//
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