ID A0A1H2FPH8_9FLAO Unreviewed; 385 AA.
AC A0A1H2FPH8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=SAMN04487762_1755 {ECO:0000313|EMBL:SDU09257.1};
OS Polaribacter sp. Hel1_33_78.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1336804 {ECO:0000313|EMBL:SDU09257.1, ECO:0000313|Proteomes:UP000198843};
RN [1] {ECO:0000313|EMBL:SDU09257.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hel1_33_78 {ECO:0000313|EMBL:SDU09257.1};
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; LT629794; SDU09257.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2FPH8; -.
DR STRING; 1336804.SAMN04487762_1755; -.
DR OrthoDB; 9807797at2; -.
DR Proteomes; UP000198843; Chromosome i.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
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; 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; 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:SDU09257.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198843};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}.
FT DOMAIN 38..175
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT DOMAIN 295..384
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 385 AA; 42611 MW; D7A87300D92DC6BA CRC64;
MKIYIYSFII VILVVGCTPA KYNGLKEGLY AEIQTNKGDV LLELYAEDAP MTVANFVSLA
EGTNTKVTDS IQGKKYFDGI RFHRVVNNFI IQGGDPTETG RGTAGYRFGD EFTKDINGKL
LHIHGDAGML SMANGGPESN GSQFFITHRA IPHLDGKHTV FGKTVVNSLQ LNTLKLQIKD
SLKRKNAIDS LRMSVVNSIQ QFDTIFTVKI IRIGAVANAF KAGEVFDNEF IKYAEGKKDR
NKKAKDADEE RFSKYLENRT TFLAKMNESK AIKTASGLRI LKLTSNPSGK KVVTNKPIKA
HFTLYIADGT KIQSTLDSGN PFVFQLDDAE KPMITGFKEG AATLRVGEKA RLFIPYYIGF
GEAKYGPFPA KSDLVFEVEI LEIGE
//
