ID A0A1X0DEJ3_9MYCO Unreviewed; 297 AA.
AC A0A1X0DEJ3;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=BST26_09745 {ECO:0000313|EMBL:ORA70788.1};
OS Mycolicibacterium insubricum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=444597 {ECO:0000313|EMBL:ORA70788.1, ECO:0000313|Proteomes:UP000192801};
RN [1] {ECO:0000313|EMBL:ORA70788.1, ECO:0000313|Proteomes:UP000192801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45130 {ECO:0000313|EMBL:ORA70788.1,
RC ECO:0000313|Proteomes:UP000192801};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (DEC-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|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:ORA70788.1}.
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DR EMBL; MVHS01000018; ORA70788.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0DEJ3; -.
DR STRING; 444597.BST26_09745; -.
DR OrthoDB; 5507614at2; -.
DR Proteomes; UP000192801; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF3; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE B-RELATED; 1.
DR PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 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, ECO:0000313|EMBL:ORA70788.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000192801};
KW Rotamase {ECO:0000256|RuleBase:RU363019};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 135..296
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000259|PROSITE:PS50072"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 297 AA; 31158 MW; F48F2F5F752EEFFF CRC64;
MPTNEQRRAA AKRKLDRQLE RREAKAKRQR TLAIGAAVLA VVVAAVASGT FWWLHREDNP
GNSAEVDPTT VAEATANAEP ENAGTGSLPK FTPSANLGGN CQYPATVKES AAKANKPPRT
GKVPTDPAQV SVSMSTTAGN VGLMLDNAKS PCTVNSFVSL AQQGYFDDTP CHRLTTSPSL
SVLQCGDPGG TGSGGPGYKF GNEYPTDQYP AGSPNLDKPV TYPRGTLAMA NAGPNTNGSQ
FFLVYKDSQL PPQYTVFGTI DETGLATLDK IGAEGTANGT PDGKPKTDVK IKSVRVD
//
