ID A0A3R8NA99_9CAUL Unreviewed; 324 AA.
AC A0A3R8NA99;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Parvulin-like PPIase {ECO:0000256|ARBA:ARBA00018370};
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase plp {ECO:0000256|ARBA:ARBA00030642};
DE AltName: Full=Rotamase plp {ECO:0000256|ARBA:ARBA00031484};
GN ORFNames=EIK80_05430 {ECO:0000313|EMBL:RRN65016.1};
OS Caulobacter sp. 602-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=2492472 {ECO:0000313|EMBL:RRN65016.1, ECO:0000313|Proteomes:UP000268773};
RN [1] {ECO:0000313|EMBL:RRN65016.1, ECO:0000313|Proteomes:UP000268773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=602-1 {ECO:0000313|EMBL:RRN65016.1,
RC ECO:0000313|Proteomes:UP000268773};
RA Gao J., Sun J.;
RT "The genome of Caulobacter sp 602-1.";
RL Submitted (NOV-2018) 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:RRN65016.1}.
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; RRYI01000002; RRN65016.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R8NA99; -.
DR OrthoDB; 14196at2; -.
DR Proteomes; UP000268773; Unassembled WGS sequence.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.1040; -; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR023058; PPIase_PpiC_CS.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR PANTHER; PTHR47245:SF1; FOLDASE PROTEIN PRSA; 1.
DR PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR Pfam; PF13145; Rotamase_2; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:RRN65016.1};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..324
FT /note="Parvulin-like PPIase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018640899"
FT DOMAIN 150..240
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 287..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 324 AA; 34713 MW; EBFABA93E10C5660 CRC64;
MALNSTLRRV GMISAIACAL LLAACGQNKV ADKPPEPGDT AVARVNGQVI WASDVKREAV
AQGLISEGEP LDISSEVFRQ RLDEVIDQKL LAAEASKRKI DKDPVAQRRL AAARERILGD
MLVEGVVEKA VTEDAIRKLY AEQQKLSKRS EEIRARQIIV GSQAEADSIK KLLASGASFD
ALAMERSTDQ ATRFNGGDLG YFTLDVMPEP YGVALKDAQK GALVGPFAAE GGWVIVKVED
KRTEEPITLE AARPQIVRFL TYDQVRDILE KLRGSAKVEM LIGKPQDVSG ATGAQEPASA
PAELQGGAPA SAPPPAQPVQ PAKK
//
