ID A0A2A3UIK4_9SPHI Unreviewed; 371 AA.
AC A0A2A3UIK4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=CNR22_22625 {ECO:0000313|EMBL:PBQ34980.1};
OS Sphingobacteriaceae bacterium.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae.
OX NCBI_TaxID=2021370 {ECO:0000313|EMBL:PBQ34980.1, ECO:0000313|Proteomes:UP000217505};
RN [1] {ECO:0000313|EMBL:PBQ34980.1, ECO:0000313|Proteomes:UP000217505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH-48 {ECO:0000313|EMBL:PBQ34980.1,
RC ECO:0000313|Proteomes:UP000217505};
RA Choi A.;
RT "Draft genome sequence of sphingobacterial strain SH-48, isolated from
RT freshwater in Korea.";
RL Submitted (SEP-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};
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:PBQ34980.1}.
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; NVQB01000001; PBQ34980.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3UIK4; -.
DR OrthoDB; 9807797at2; -.
DR Proteomes; UP000217505; Unassembled WGS sequence.
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.
PE 4: Predicted;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000313|EMBL:PBQ34980.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000217505};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}.
FT DOMAIN 44..198
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT DOMAIN 281..371
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 371 AA; 39613 MW; 22139D8867E5CF03 CRC64;
MISALSVLTF SAEAQKKAKL SKADKEFLAK QADGIYAKLE TTRGDIYTQL EFKQVPMTVA
NFVGLSEGTI KNSAKGAGVP YYDGIKFHRV IPGFMIQGGD PMGTGGGDPG YSFEDEFLPN
SELAKNGYKR GVMAMANRGP NTNGSQFFLM HADYGLPYSY TIFGHIVKGI EVVDSIATAP
KNGGDMPNVD QTIKHVTILR KGKEAEAFDA AKVFETERAA APAKAAARIK AEEEAAKAKQ
AGAAAEATKI LNEKYSSAQV TASGLRTMIE KTGEGAAIKQ ADKVVLHCTG TLIDGTKFWS
SYDGEGKPLE VSLGVSPRLI PGMEEGIMLL KQGGKAKLII PPNIGYGERG QPPVIPGNSW
LVFDVEVLKV N
//
