ID J9ZD46_LEPFM Unreviewed; 289 AA.
AC J9ZD46;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Parvulin-like peptidyl-prolyl isomerase {ECO:0000313|EMBL:AFS54620.1};
GN OrderedLocusNames=LFML04_2431 {ECO:0000313|EMBL:AFS54620.1};
OS Leptospirillum ferriphilum (strain ML-04).
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Leptospirillum.
OX NCBI_TaxID=1048260 {ECO:0000313|EMBL:AFS54620.1, ECO:0000313|Proteomes:UP000006177};
RN [1] {ECO:0000313|EMBL:AFS54620.1, ECO:0000313|Proteomes:UP000006177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ML-04 {ECO:0000313|EMBL:AFS54620.1,
RC ECO:0000313|Proteomes:UP000006177};
RX PubMed=22203551; DOI=10.1007/s12275-011-1099-9;
RA Mi S., Song J., Lin J., Che Y., Zheng H., Lin J.;
RT "Complete genome of Leptospirillum ferriphilum ML-04 provides insight into
RT its physiology and environmental adaptation.";
RL J. Microbiol. 49:890-901(2011).
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; CP002919; AFS54620.1; -; Genomic_DNA.
DR RefSeq; WP_014962123.1; NC_018649.1.
DR AlphaFoldDB; J9ZD46; -.
DR STRING; 1048260.LFML04_2431; -.
DR KEGG; lfi:LFML04_2431; -.
DR PATRIC; fig|1048260.3.peg.2641; -.
DR HOGENOM; CLU_917633_0_0_0; -.
DR Proteomes; UP000006177; Chromosome.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.1040; -; 1.
DR Gene3D; 6.10.140.970; -; 1.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR PANTHER; PTHR47245:SF2; SLR0208 PROTEIN; 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; PS50198; PPIC_PPIASE_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:AFS54620.1};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..289
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007919591"
FT DOMAIN 130..220
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 289 AA; 32363 MW; DFEC499E434E6B05 CRC64;
MSRKPLKYAS LFLLPILLSS CHKSSAPLPD SVLAKVGNTT ISQGDLKKKL DSMGLASSKD
PNVTSELLNQ MVDNSLLAMQ ARKEGLDKTP EFKKKMHAYE TKLLRKALLK KDVDDKVKVT
DSDIVNYYNK HQKDIKQPGY VDVRQVVFPD EKTAKRDFPL LKKKGGFKKV TKMFKGGPVG
KIYEGTVPPK FVSFFFGVPE GSITGPIPLK DGIHYFKIDR SVKGVQLTLD QAREGIRNYL
RNRQNKTIYQ TLVNHLRSTT TVQINNKALV SMISRAANAK SPAPDQIKK
//