ID A0A2A7UWM3_COMTR Unreviewed; 261 AA.
AC A0A2A7UWM3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Peptidylprolyl isomerase {ECO:0000313|EMBL:PEH89690.1};
GN ORFNames=CRM82_14755 {ECO:0000313|EMBL:PEH89690.1};
OS Comamonas terrigena.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=32013 {ECO:0000313|EMBL:PEH89690.1, ECO:0000313|Proteomes:UP000220246};
RN [1] {ECO:0000313|Proteomes:UP000220246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_394 {ECO:0000313|Proteomes:UP000220246};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC {ECO:0000256|ARBA:ARBA00007656}.
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:PEH89690.1}.
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DR EMBL; PDEA01000001; PEH89690.1; -; Genomic_DNA.
DR RefSeq; WP_066532775.1; NZ_UIGV01000001.1.
DR AlphaFoldDB; A0A2A7UWM3; -.
DR STRING; 1219032.GCA_001515545_00307; -.
DR GeneID; 80801882; -.
DR OrthoDB; 14196at2; -.
DR Proteomes; UP000220246; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
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; PS50198; PPIC_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:PEH89690.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000220246};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..261
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012495862"
FT DOMAIN 131..222
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 162..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 261 AA; 28883 MW; 5805D9225E63A63A CRC64;
MKKQLLSSLV AAALLGTMAF SATAQNLAIV NGKPVPKARA DVLKQQLERS GRPVSAEMEE
QIKEEVIARE IFLQEAGRRG LAASPGFRQQ MELNRENVLI RELFIDFQKK NPVTDAEIKA
EYDKFAAANE GKEYHAAHIL VDSEERAKAI IAEVKGGKKF EDIAKKESKD PGSGAQGGDL
GWSNPGSYVP EFSEAMLKLN KGEMTSTPVK TQFGWHVIRV IETRQAQLPA LDDVKPQIAQ
QLEQQKLMQF QDGLRAKAKV Q
//
