ID A0A2U2J9V8_9FLAO Unreviewed; 309 AA.
AC A0A2U2J9V8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN ORFNames=DIS07_07740 {ECO:0000313|EMBL:PWG05128.1};
OS Polaribacter aquimarinus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=2100726 {ECO:0000313|EMBL:PWG05128.1, ECO:0000313|Proteomes:UP000245670};
RN [1] {ECO:0000313|EMBL:PWG05128.1, ECO:0000313|Proteomes:UP000245670}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZY113 {ECO:0000313|EMBL:PWG05128.1,
RC ECO:0000313|Proteomes:UP000245670};
RA Lu D.;
RT "Polaribacter aquimarinus sp. nov., isolated from sediment in a sediment of
RT sea.";
RL Submitted (MAY-2018) 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:PWG05128.1}.
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DR EMBL; QFFG01000003; PWG05128.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2J9V8; -.
DR OrthoDB; 9807797at2; -.
DR Proteomes; UP000245670; 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:UP000245670};
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 221..309
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 309 AA; 33412 MW; 5833C1F344FD7F10 CRC64;
MNNGIYAKFT TSKGDILVQL EYEKTPGTVG NFVALSEGNL ENSAKSQGTP YYDGLKFHRV
IPDFMIQGGC PLGTGTGNPG YKFDDEFHPD LKHDAPGKLA MANSGPATNG SQFYITHVPT
PWLDNKHTVF GSVIEGQDVV DAVAQGDDMK VEIVRVGADA ENFNAVEAFR KFEGAREERE
AEEKRKQKEL LDKVAAGYDE TASGLRYQIL QKGNGKQATK GAGVSVHYKG QLLDGTVFDS
SYKRKQPIDF NVGVGQVISG WDEGIQLLQV GDKARFVIPS NLAYGSAGAG GVIPPNATLI
FDVELMDVK
//
