ID A0A1M6GGX7_9FLAO Unreviewed; 310 AA.
AC A0A1M6GGX7;
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=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN ORFNames=SAMN05444363_2611 {ECO:0000313|EMBL:SHJ09205.1};
OS Flavobacterium terrae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=415425 {ECO:0000313|EMBL:SHJ09205.1, 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, ECO:0000256|RuleBase:RU003915};
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC {ECO:0000256|RuleBase:RU003915}.
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DR EMBL; FQZI01000005; SHJ09205.1; -; Genomic_DNA.
DR RefSeq; WP_073311936.1; NZ_FQZI01000005.1.
DR AlphaFoldDB; A0A1M6GGX7; -.
DR STRING; 415425.SAMN05444363_2611; -.
DR OrthoDB; 9807797at2; -.
DR Proteomes; UP000184488; 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:UP000184488};
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; 33544 MW; FB4C339428C244FA CRC64;
MQDGIYAKFN TSKGSILVKL THDLTPGTVG NFVGLAEGNL ENSVKPQGQK YYDGLKFHRV
IPDFMIQGGC PLGTGTGDAG YKFDDEFHPS LRHDKPGILS MANAGPGTNG SQFFITHVAT
PWLDGKHSVF GHVVEGQDVV DAVAQGDALE SVEIIRVGAD AENWNAIEAF RTFEGSRLKR
IEEAKRQAEE AMEKLAAGFE KTESGLRYKI IQKGNGKQAE AGKTVSVHYQ GSLENGKTFD
SSYARKKPIE FPLGKGHVIE GWDEGIALLQ VGDKARFVIP AYLGYGDRGA GGVIPPNATL
VFDVELMDVK
//
