ID A0A2M9BYU1_9MICO Unreviewed; 324 AA.
AC A0A2M9BYU1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=CLV54_0905 {ECO:0000313|EMBL:PJJ63247.1};
OS Compostimonas suwonensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Compostimonas.
OX NCBI_TaxID=1048394 {ECO:0000313|EMBL:PJJ63247.1, ECO:0000313|Proteomes:UP000230161};
RN [1] {ECO:0000313|EMBL:PJJ63247.1, ECO:0000313|Proteomes:UP000230161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25625 {ECO:0000313|EMBL:PJJ63247.1,
RC ECO:0000313|Proteomes:UP000230161};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-2017) 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 -!- 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:PJJ63247.1}.
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DR EMBL; PGFB01000002; PJJ63247.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9BYU1; -.
DR OrthoDB; 25996at2; -.
DR Proteomes; UP000230161; 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; PTHR10516:SF466; FK506-BINDING PROTEIN 59; 1.
DR PANTHER; PTHR10516; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR Pfam; PF00254; FKBP_C; 2.
DR SUPFAM; SSF54534; FKBP-like; 2.
DR PROSITE; PS50059; FKBP_PPIASE; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW ProRule:PRU00277}; Reference proteome {ECO:0000313|Proteomes:UP000230161};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..324
FT /note="peptidylprolyl isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039670809"
FT DOMAIN 77..167
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 223..316
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REGION 23..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 324 AA; 32244 MW; 2B132ED04E3B1EFB CRC64;
MRKTSALIVT AGLLAVALSA CSPSSGSTGD CTPEASSGAT SDAVTVSGSL GSNPTVDFPT
PLKTKTTEVT EVIPGSGDVV KSGQKVATEM TVFNGTTGES IQDTGAAAFV LGQTITGITD
GLVCSTTGSR VVVAVPPEDG FGTEGNAQLG ISGTDTLVFV FDVTKSYLSR ADGADQPAQA
GFPSVVTAPE TGQPGITIPA GDAPTELKVA VLKKGGGEPV VEGDSVTVHY TGVIWDSKTV
FDSSWESGSP ATFLAADGSK VQGGVIPGFA NALIGQTVGS QIIAIIPPDQ AYGEAGNQSV
PANATLVFVV DILGVDPAPA APQQ
//
