ID A0A1U7LYN3_9FIRM Unreviewed; 249 AA.
AC A0A1U7LYN3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN ORFNames=BIV18_02550 {ECO:0000313|EMBL:OLR64503.1};
OS Peptoniphilus porci.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=1261639 {ECO:0000313|EMBL:OLR64503.1, ECO:0000313|Proteomes:UP000187166};
RN [1] {ECO:0000313|EMBL:OLR64503.1, ECO:0000313|Proteomes:UP000187166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35-6-1 {ECO:0000313|EMBL:OLR64503.1,
RC ECO:0000313|Proteomes:UP000187166};
RX PubMed=27613689;
RA Trachsel J., Bayles D.O., Looft T., Levine U.Y., Allen H.K.;
RT "Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate
RT Transferases and Their Diversity in the Proximal Colon of Swine.";
RL Appl. Environ. Microbiol. 82:6788-6798(2016).
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};
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:OLR64503.1}.
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DR EMBL; MJIH01000001; OLR64503.1; -; Genomic_DNA.
DR RefSeq; WP_075659146.1; NZ_MJIH01000001.1.
DR AlphaFoldDB; A0A1U7LYN3; -.
DR STRING; 1465756.BIV18_02550; -.
DR OrthoDB; 14196at2; -.
DR Proteomes; UP000187166; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.1040; -; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR023058; PPIase_PpiC_CS.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR PANTHER; PTHR47245:SF1; FOLDASE PROTEIN PRSA; 1.
DR PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR Pfam; PF13616; Rotamase_3; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW ProRule:PRU00278}; Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 114..203
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 249 AA; 28556 MW; 71687CFABA829846 CRC64;
MDKDKLLAEV NGKKITGVDY NLFIDSLNPQ LKQYFGGEEI NKEVVNELVY QALLYQDAIE
KGMDKNDEFI QVLEKTKESM LKTYALGKLL EKVTVTEDEV KKFYEDNKDA FKEGESANAS
HILVEEEDKA REIYEKIKSG EDFASLAKDF STCPSKEKGG ELGTFTRGQM VKEFEDAVFA
NEVGTVTKPV KTQFGYHIIK INDKNKGRDL AFDEVKDKIA TQIRRQKEQE IYSKKIAELK
DKYEVKMDI
//
