ID A0A1M6GL27_9FLAO Unreviewed; 368 AA.
AC A0A1M6GL27;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=SAMN05444363_2671 {ECO:0000313|EMBL:SHJ10648.1};
OS Flavobacterium terrae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=415425 {ECO:0000313|EMBL:SHJ10648.1, ECO:0000313|Proteomes:UP000184488};
RN [1] {ECO:0000313|Proteomes:UP000184488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18829 {ECO:0000313|Proteomes:UP000184488};
RA Varghese N., Submissions S.;
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};
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DR EMBL; FQZI01000005; SHJ10648.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6GL27; -.
DR STRING; 415425.SAMN05444363_2671; -.
DR OrthoDB; 9807797at2; -.
DR Proteomes; UP000184488; 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:SHJ10648.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184488};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..368
FT /note="peptidylprolyl isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012206601"
FT DOMAIN 38..170
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT DOMAIN 254..360
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 368 AA; 39615 MW; 764804CDA9291ADB CRC64;
MNRMTSLFLS FFALLFSCNS GDQNLPDGMY AELETSKGKI VLQLEYEKTP VTVANFVALA
EGKNTMVNEK YSGKPFYDGL KFHRVIADFM IQGGDPDGNG SGGPGYKFKD EIVPDLKHTG
PGILSMANAG PGTNGSQFFI THKATPWLDG RHTVFGHVVT GQDVVNTIAQ DDLIKKVTII
RKGAKAKKFD AAKIFKDHVQ NQIAEQKANE AKYAKVKADK VAAFAQAKAS GTKTESGLVY
NIIQKGSGKK PVAGSTVYVN YAGYFEDGNL FDSSYEDVNK AYGKWDANRA AQKGYQPFPF
QAGNKSGLIP GFLEGLEKMN IGDKALLFIP SNLGYGAQGA GGVIPPNTNL VFELELLETA
PGTPAVAK
//
