ID A0A1V2YK40_9FIRM Unreviewed; 188 AA.
AC A0A1V2YK40;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363019};
DE Short=PPIase {ECO:0000256|RuleBase:RU363019};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU363019};
GN ORFNames=BEN18_02570 {ECO:0000313|EMBL:OOB79907.1};
OS Epulopiscium sp. Nuni2H_MBin001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Candidatus Epulonipiscium.
OX NCBI_TaxID=1884656 {ECO:0000313|EMBL:OOB79907.1, ECO:0000313|Proteomes:UP000189057};
RN [1] {ECO:0000313|EMBL:OOB79907.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nuni2H_MBin001 {ECO:0000313|EMBL:OOB79907.1};
RA Ngugi D.K., Miyake S., Stingl U.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides. {ECO:0000256|ARBA:ARBA00002388,
CC ECO:0000256|RuleBase:RU363019}.
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|RuleBase:RU363019};
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000256|RuleBase:RU363019}.
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:OOB79907.1}.
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DR EMBL; MDJM01000003; OOB79907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V2YK40; -.
DR STRING; 1884656.BEN18_02570; -.
DR Proteomes; UP000189057; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR CDD; cd00317; cyclophilin; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
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; PF00160; Pro_isomerase; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|RuleBase:RU363019};
KW Reference proteome {ECO:0000313|Proteomes:UP000189057};
KW Rotamase {ECO:0000256|RuleBase:RU363019}.
FT DOMAIN 16..172
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 188 AA; 21000 MW; 6DCBC12FDC33D0EC CRC64;
MYYSGIIFAS DDSNNYPIVT ITFDNNKEIK IELYPNEAPN TVNNFIDLAN QGFYEYTFVS
KIIPGYFVQA GDPIGNGFGY PGYYIESECK FNGINNKISL TRGTVAMARG EAFDTEGSQF
FILTEDARHL TGQYSAFGSV IEGMEVIDKL GTVELDNDYM PQDPIFITDI SVELNGYEPE
SPEVITAY
//
