ID A0A1I6T4J6_9BACI Unreviewed; 226 AA.
AC A0A1I6T4J6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-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=SAMN05421668_11268 {ECO:0000313|EMBL:SFS84106.1};
OS Halolactibacillus miurensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halolactibacillus.
OX NCBI_TaxID=306541 {ECO:0000313|EMBL:SFS84106.1, ECO:0000313|Proteomes:UP000199139};
RN [1] {ECO:0000313|EMBL:SFS84106.1, ECO:0000313|Proteomes:UP000199139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17074 {ECO:0000313|EMBL:SFS84106.1,
RC ECO:0000313|Proteomes:UP000199139};
RA de Groot N.N.;
RL Submitted (OCT-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FPAI01000012; SFS84106.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6T4J6; -.
DR STRING; 306541.SAMN05421668_11268; -.
DR OrthoDB; 9807797at2; -.
DR Proteomes; UP000199139; 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; 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 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; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|RuleBase:RU363019, ECO:0000313|EMBL:SFS84106.1};
KW Rotamase {ECO:0000256|RuleBase:RU363019};
KW Signal {ECO:0000256|RuleBase:RU363019}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU363019"
FT CHAIN 21..226
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /evidence="ECO:0000256|RuleBase:RU363019"
FT /id="PRO_5039748412"
FT DOMAIN 70..213
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
SQ SEQUENCE 226 AA; 24578 MW; CC336EABD4DEA783 CRC64;
MKKIALLLSS VLLIAIVVGC ADTATDEPIE DTPEDTTLTF EEEQTAFYEQ YPEVTDNPIV
TIEMATGETI TLELYPHTAP NTVANFIALI EDGFYDGVIF HRIIEDFMIQ GGDPQGNGLG
GPDYSIPGEF NSNGFDNDLV HEPGVISMAR SQSPDSAGSQ FFIMHKAATH LDGEYAGFGQ
VTEGMEVVNK LAQVETGPND VPVEEQQIKT MTVDTKGVDY PDPLKK
//
