ID A0A1H4IQD6_9FLAO Unreviewed; 346 AA.
AC A0A1H4IQD6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
GN ORFNames=SAMN04489761_0056 {ECO:0000313|EMBL:SEB35422.1};
OS Tenacibaculum sp. MAR_2009_124.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=1250059 {ECO:0000313|EMBL:SEB35422.1, ECO:0000313|Proteomes:UP000199366};
RN [1] {ECO:0000313|EMBL:SEB35422.1, ECO:0000313|Proteomes:UP000199366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mar_2009_124 {ECO:0000313|EMBL:SEB35422.1,
RC ECO:0000313|Proteomes:UP000199366};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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};
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DR EMBL; FNSF01000001; SEB35422.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4IQD6; -.
DR STRING; 1250059.SAMN04489761_0056; -.
DR OrthoDB; 9807797at2; -.
DR Proteomes; UP000199366; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR CDD; cd00317; cyclophilin; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR PANTHER; PTHR45625:SF4; PEPTIDYLPROLYL ISOMERASE DOMAIN AND WD REPEAT-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000313|EMBL:SEB35422.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199366};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}.
FT DOMAIN 38..176
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT DOMAIN 258..345
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 346 AA; 38853 MW; A5A8E1E3AD0C417A CRC64;
MKLFKILFII TIVFASCKTA KYPNLDNGLY ADIQTNRGDI LIKLHEKEVP MTVANFVSLA
EGSNPKMTDS LKGKPYFDGT KFHRVISDFM IQGGDITGTG RGNAGYRFAD EFPLNEKGEL
IYKHDKKGVL SMANSGKSTN SSQFFITHKA TPWLDGKHTI FGQVKVGQNI VDTIQKDDFI
NRVDIIRIGK EAKKFKAEEI FQFELTNVEQ REEERKKKLE EAKARFQKEK GIENAVSTDS
GLKILSIQKG KGKKVNPAIP TTVHYTLYLT DGKKIASSID ENKPFVFTID KQSLIAGWKE
GVKTMREGDK SRFFIPYYLG YGDKGVGPIP SKSDLVFEVE VLKVGK
//
