ID U2PET7_9ACTN Unreviewed; 356 AA.
AC U2PET7;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
GN ORFNames=HMPREF0682_1543 {ECO:0000313|EMBL:ERK49000.1};
OS Propionibacterium acidifaciens F0233.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionibacterium.
OX NCBI_TaxID=553198 {ECO:0000313|EMBL:ERK49000.1, ECO:0000313|Proteomes:UP000017052};
RN [1] {ECO:0000313|EMBL:ERK49000.1, ECO:0000313|Proteomes:UP000017052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0233 {ECO:0000313|EMBL:ERK49000.1,
RC ECO:0000313|Proteomes:UP000017052};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (AUG-2013) 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};
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC {ECO:0000256|ARBA:ARBA00006577}.
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:ERK49000.1}.
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DR EMBL; ACVN02000334; ERK49000.1; -; Genomic_DNA.
DR RefSeq; WP_021798963.1; NZ_ACVN02000334.1.
DR AlphaFoldDB; U2PET7; -.
DR OrthoDB; 25996at2; -.
DR Proteomes; UP000017052; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 2.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR PANTHER; PTHR43811:SF19; 39 KDA FK506-BINDING NUCLEAR PROTEIN; 1.
DR PANTHER; PTHR43811; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKPA; 1.
DR Pfam; PF00254; FKBP_C; 2.
DR SUPFAM; SSF54534; FKBP-like; 2.
DR PROSITE; PS50059; FKBP_PPIASE; 2.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000313|EMBL:ERK49000.1};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}.
FT DOMAIN 116..205
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 264..353
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REGION 37..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 356 AA; 35650 MW; 4068F93A6BD50840 CRC64;
MPVHSSGSVP AARALSRRRV AAALLVPVVL LGAAGCGKSE ASSDQSSSAS APSSASPEAS
ESTSQAPATI IDNLDQIDVE GEPGQAPTVS ASWPLGVNET MSKVLVPGDG AEVTEGGSVE
VNYHGVDGRT GDVFDESYSS GKTATFSLGQ VIAGFSKGLT GKHVGDRVLL GVTGADGYDS
SGGASSAGIE VGDSLFFVVD IVSTTLTAPS GDTVPVDDPN LPAVTWDNGV NNPSVSIPSG
VDAPGELKVQ PLIKGNGAQI ADAGATVTVN YLEVAYSDGH VIDSTYGDGN PTPQSGALGS
LIDGWQQGLV GQTVGSRVLL VVPGSLAYPN GNASPAIDPN ATLVFVVDIL YQQTSS
//
