ID A0A1M5SNH3_9FLAO Unreviewed; 310 AA.
AC A0A1M5SNH3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN ORFNames=SAMN05444148_1917 {ECO:0000313|EMBL:SHH40000.1};
OS Winogradskyella jejuensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=1089305 {ECO:0000313|EMBL:SHH40000.1, ECO:0000313|Proteomes:UP000184522};
RN [1] {ECO:0000313|EMBL:SHH40000.1, ECO:0000313|Proteomes:UP000184522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25330 {ECO:0000313|EMBL:SHH40000.1,
RC ECO:0000313|Proteomes:UP000184522};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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, ECO:0000256|RuleBase:RU003915};
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC {ECO:0000256|RuleBase:RU003915}.
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DR EMBL; FQWS01000002; SHH40000.1; -; Genomic_DNA.
DR RefSeq; WP_073085864.1; NZ_FQWS01000002.1.
DR AlphaFoldDB; A0A1M5SNH3; -.
DR STRING; 1089305.SAMN05444148_1917; -.
DR OrthoDB; 9807797at2; -.
DR Proteomes; UP000184522; 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 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; 33169 MW; 96C0E4BD5CE67F54 CRC64;
MQDGLYAKFN TSKGEILVNL EFEKTPGTVG NFVALAEGNL ENSAKPQGTP YYDGLKFHRV
IPDFMIQGGC PLGTGTGNPG YKFDDEIHPD LKHDGPGVLS MANAGPGTNG SQFFITHIAT
DWLDGKHTVF GNVVEGQDVV DTIAQGDAIE SLEIVRVGEA AENFNAVEAF RVFEGAREKR
VAAEREARRA ELDKLAAGFE ETASGLRYQI LQKGDGKKAK KGNMVSVHYK GQLADGTVFD
SSYKRNAPLD FQVGVGQVIS GWDEGICLLN VGDKARLVIP SDLGYGSAGA GGVIPPNATL
VFDVELMDVK
//
