ID A0A0N1N3S0_9PROT Unreviewed; 301 AA.
AC A0A0N1N3S0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
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};
DE Flags: Precursor;
GN ORFNames=GLUCOINTEAF2_0201295 {ECO:0000313|EMBL:KPH85140.1};
OS Komagataeibacter intermedius AF2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Komagataeibacter.
OX NCBI_TaxID=1458464 {ECO:0000313|EMBL:KPH85140.1, ECO:0000313|Proteomes:UP000031553};
RN [1] {ECO:0000313|EMBL:KPH85140.1, ECO:0000313|Proteomes:UP000031553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF2 {ECO:0000313|EMBL:KPH85140.1,
RC ECO:0000313|Proteomes:UP000031553};
RA Santos R.A., Berretta A.A., Barud H.S., Ribeiro S.J., Gonzalez-Garcia L.N.,
RA Zucchi T.D., Goldman G.H., Riano-Pachon D.M.;
RT "Draft Genome Sequence of Komagataeibacter intermedius Strain AF2, Isolated
RT from Kombucha Tea.";
RL Submitted (JUL-2015) 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:KPH85140.1}.
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DR EMBL; JUFX02000258; KPH85140.1; -; Genomic_DNA.
DR RefSeq; WP_039736351.1; NZ_JUFX02000258.1.
DR AlphaFoldDB; A0A0N1N3S0; -.
DR Proteomes; UP000031553; 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; PF13616; Rotamase_3; 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:KPH85140.1};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..301
FT /note="Parvulin-like PPIase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007779111"
FT DOMAIN 154..246
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 301 AA; 32258 MW; 1675383096B11088 CRC64;
MRTISPAKAV ATMALLASSF IVPPAFAASP APAAAKPAAP ATADQNPLLA SVNGQDIRLN
DVRQAMATMP EQLRKLPDNI IVPILLNQLV DQRAIQVAAA KAGLDKQPDV QQQMQQAAQN
ALQNAYLSAQ VAPTLTDDAV KAYYDKNYAN KPGAEEIHAR HILVQTEAEA NDVIKQLKGG
ADFGQLATKL SKDPGSAKQN GGDLGWFKKG DMLPTFWDAA SAMQPNTFSQ TPVHTQYGWH
VIQVLGKRTA PTPTLDATRD QIRQKLIQEG VQKAVSNALS QVKVVRYGPD GKPLPEQPAA
H
//
