ID A0A506PKX4_9FLAO Unreviewed; 310 AA.
AC A0A506PKX4;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 08-NOV-2023, entry version 13.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN ORFNames=FJ651_11495 {ECO:0000313|EMBL:TPV32920.1};
OS Paucihalobacter ruber.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Paucihalobacter.
OX NCBI_TaxID=2567861 {ECO:0000313|EMBL:TPV32920.1, ECO:0000313|Proteomes:UP000317332};
RN [1] {ECO:0000313|EMBL:TPV32920.1, ECO:0000313|Proteomes:UP000317332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWB-1 {ECO:0000313|EMBL:TPV32920.1,
RC ECO:0000313|Proteomes:UP000317332};
RA Wu S.;
RT "Flavobacteriaceae Paucihalobacterium erythroidium CWB-1, complete
RT genome.";
RL Submitted (JUN-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}.
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:TPV32920.1}.
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DR EMBL; VHIQ01000005; TPV32920.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A506PKX4; -.
DR OrthoDB; 9807797at2; -.
DR Proteomes; UP000317332; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
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.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000256|RuleBase:RU003915};
KW Reference proteome {ECO:0000313|Proteomes:UP000317332};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}.
FT DOMAIN 14..145
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT DOMAIN 222..310
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 310 AA; 33521 MW; 7DE70CC90E389D24 CRC64;
MNNGLYAKFN TSKGTITVNL TFDKTPGTVG NFVALAEGNM ENSAKPQGKP YYDGLKFHRV
IPDFMIQGGC PLGTGTGNPG YKFDDEFHPD LKHDGPGVLS MANAGPGTNG SQFFITHVET
PWLDNNHTVF GKVIEGQEVV DAIAQGDQIN TLEIIRVGDA AENFNAIEAF RTFEGAREKR
LEAERTAIAA QLDKVSAGFS ETKSGLRYQI IQKGSGKQPQ KGNKVAVHYK GQLMDGTVFD
SSYKRNQPLE FQVGVGQVIE GWDEGILLLN EGDKARLVIP SNLGYGSRGA GGVIPPNANL
IFDVELVKVK
//
