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Entry: A0A2S2DT74_9BACT
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ID   A0A2S2DT74_9BACT        Unreviewed;       287 AA.
AC   A0A2S2DT74;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN   Name=fkpA {ECO:0000313|EMBL:AWL08499.1};
GN   ORFNames=EWU22_04950 {ECO:0000313|EMBL:TBH75899.1}, HME7025_00627
GN   {ECO:0000313|EMBL:AWL08499.1};
OS   Aquirufa nivalisilvae.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Aquirufa.
OX   NCBI_TaxID=2516557 {ECO:0000313|EMBL:AWL08499.1, ECO:0000313|Proteomes:UP000245468};
RN   [1] {ECO:0000313|Proteomes:UP000245468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HME7025 {ECO:0000313|Proteomes:UP000245468};
RA   Kim H., Kang H., Joh K.;
RT   "Pseudarcicella sp. HME7025 Genome sequencing and assembly.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AWL08499.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HME7025 {ECO:0000313|EMBL:AWL08499.1};
RX   PubMed=31433289;
RA   Kim H., Kang H., Joh K.;
RT   "Allopseudarcicella aquatilis gen. nov., sp. nov., isolated from
RT   freshwater.";
RL   Int. J. Syst. Evol. Microbiol. 69:3574-3580(2019).
RN   [3] {ECO:0000313|EMBL:TBH75899.1, ECO:0000313|Proteomes:UP000292948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=59G-WUEMPEL {ECO:0000313|EMBL:TBH75899.1,
RC   ECO:0000313|Proteomes:UP000292948};
RA   Pitt A.;
RT   "Genome of a new Bacteroidetes strain.";
RL   Submitted (FEB-2019) 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; CP029346; AWL08499.1; -; Genomic_DNA.
DR   EMBL; SEWX01000002; TBH75899.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S2DT74; -.
DR   KEGG; psez:HME7025_00627; -.
DR   OrthoDB; 9814548at2; -.
DR   Proteomes; UP000245468; Chromosome.
DR   Proteomes; UP000292948; 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; 1.
DR   SUPFAM; SSF54534; FKBP-like; 2.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
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:UP000245468};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW   ProRule:PRU00277}.
FT   DOMAIN          206..287
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
SQ   SEQUENCE   287 AA;  30792 MW;  F1D66F39900371E4 CRC64;
     MRKQLIGLLS AVVFLSACNQ NKVEVIDGVK IQFHSHDDKA KKLKDGDIIT FGLVIKNSTD
     SVLQDTYKEG KPGKGMIQAP NNAPGSFKGT FENGLRLLAL GDSATILVPI DSLTKNIQAP
     LPPFLKPGSD LKYTVKVLKV QSRAEFEKEM EKEAAVNKQA AAGKLAQEPK VIADYIAKSG
     KTFQKSASGL YYSILSPGAG VAAKMGDTWT VNYRGSFVDG KEFDKGSAAE MPLGQMIPGF
     NEALTLLKKG GKGVFVIPSA LGYGDQERGP IPANSVLVFE VELLNKK
//
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