ID PLP_RICFE Reviewed; 282 AA. AC Q4UKY0; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 27-MAR-2024, entry version 84. DE RecName: Full=Parvulin-like PPIase; DE EC=5.2.1.8; DE AltName: Full=Peptidyl-prolyl cis-trans isomerase plp; DE AltName: Full=Rotamase plp; DE Flags: Precursor; GN Name=plp; OrderedLocusNames=RF_0942; OS Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=315456; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-1525 / URRWXCal2; RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248; RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E., RA Parinello H., Claverie J.-M., Raoult D.; RT "The genome sequence of Rickettsia felis identifies the first putative RT conjugative plasmid in an obligate intracellular parasite."; RL PLoS Biol. 3:1-12(2005). CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-peptidylproline (omega=180) = [protein]- CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA- CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, CC ChEBI:CHEBI:83834; EC=5.2.1.8; CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family. CC {ECO:0000305}. 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; CP000053; AAY61793.1; -; Genomic_DNA. DR AlphaFoldDB; Q4UKY0; -. DR SMR; Q4UKY0; -. DR STRING; 315456.RF_0942; -. DR KEGG; rfe:RF_0942; -. DR eggNOG; COG0760; Bacteria. DR HOGENOM; CLU_034646_1_3_5; -. DR OrthoDB; 14196at2; -. DR Proteomes; UP000008548; Chromosome. DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell. 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 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 PROSITE; PS50198; PPIC_PPIASE_2; 1. PE 3: Inferred from homology; KW Cell outer membrane; Isomerase; Membrane; Rotamase; Signal. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..282 FT /note="Parvulin-like PPIase" FT /id="PRO_0000289286" FT DOMAIN 138..231 FT /note="PpiC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00278" SQ SEQUENCE 282 AA; 31350 MW; 7B9CCEDE9FA882BF CRC64; MKKLSVIFLS VSMLSGIAFA DKDKVVATYK GGEVKESQIM KEFKPQLNLQ SGETIKNFDD FPPQDQEKLI KIYVNNLLLK EEVAKSNITS SKEFQEKLEN AKNQLAQQEL LANYIKSNIT DKMFDDEYNK YVGNLKGKEQ IKVAHILVKS QKEANNIKTK LSKGGNFTKL AEESSLDKAS ASNGGVIGYI LLNQPGQLVP EFEKKAFALK VNEVSTPVKT DFGWHIIKVL EKKPVPIPTK EEAKVTIDNI LAAEVLKKYI SDLEAKADLK IMLPKAGSKA GS //