ID B3PL06_CELJU Unreviewed; 270 AA.
AC B3PL06;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Peptidyl-prolyl cis-trans isomerase D {ECO:0000313|EMBL:ACE85429.1};
GN OrderedLocusNames=CJA_2519 {ECO:0000313|EMBL:ACE85429.1};
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211 {ECO:0000313|EMBL:ACE85429.1, ECO:0000313|Proteomes:UP000001036};
RN [1] {ECO:0000313|EMBL:ACE85429.1, ECO:0000313|Proteomes:UP000001036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107 {ECO:0000313|EMBL:ACE85429.1,
RC ECO:0000313|Proteomes:UP000001036};
RX PubMed=18556790; DOI=10.1128/JB.01701-07;
RA Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
CC -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC {ECO:0000256|ARBA:ARBA00007656}.
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DR EMBL; CP000934; ACE85429.1; -; Genomic_DNA.
DR RefSeq; WP_012488116.1; NC_010995.1.
DR AlphaFoldDB; B3PL06; -.
DR STRING; 498211.CJA_2519; -.
DR KEGG; cja:CJA_2519; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_1_3_6; -.
DR Proteomes; UP000001036; Chromosome.
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; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:ACE85429.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001036};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..270
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007910338"
FT DOMAIN 126..228
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 270 AA; 30144 MW; 5D4FCAD13ADC45CC CRC64;
MKKLLLTSAC CLAALLMGCS DSGSIASVNG KGISQEEFNA YLKFKRIPEQ DKARVDRALD
EYVNRAALAA AIEKTGKLDA AVIQAELEEF KRQMLIGRYF EEHLNGVVDD AAVRNYYAEH
QGQYESSRVH AAHILVRIDP TMGETERQAK LSTAHEIYSR LQKGEDFADL AKSYSEDKVS
GEKGGDLGWL AEGAVDPEFS KKLFSMKPGE ISEPLITPFG FHVVKMLEGP QTIKRSLESV
EGEIRYQLRN QAKATETERL VNTVKVRRQD
//
