ID   PLP_RICBR               Reviewed;         284 AA.
AC   Q1RI35;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=RBE_0898;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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}.
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DR   EMBL; CP000087; ABE04979.1; -; Genomic_DNA.
DR   RefSeq; WP_011477564.1; NC_007940.1.
DR   AlphaFoldDB; Q1RI35; -.
DR   SMR; Q1RI35; -.
DR   STRING; 336407.RBE_0898; -.
DR   EnsemblBacteria; ABE04979; ABE04979; RBE_0898.
DR   KEGG; rbe:RBE_0898; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_034646_1_3_5; -.
DR   OMA; YEQAKPT; -.
DR   OrthoDB; 1838755at2; -.
DR   Proteomes; UP000001951; 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   InterPro; IPR023058; PPIase_PpiC_CS.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR   SUPFAM; SSF109998; SSF109998; 1.
DR   PROSITE; PS01096; PPIC_PPIASE_1; 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..284
FT                   /note="Parvulin-like PPIase"
FT                   /id="PRO_0000289284"
FT   DOMAIN          139..232
FT                   /note="PpiC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
SQ   SEQUENCE   284 AA;  31790 MW;  4D33940EA0421305 CRC64;
     MKKLSIVLLS VSMLSSIAFA DNSDRVVATY TGGEVRESQI MKEFKPQLNL PSGETIKNFD
     DFPPQDQDKL IRIYVNNILL KKEVEKSNIT SSKEFQEKLE NAKNQLAQKE LLENYVKSNL
     TDKMFDDEYN KYVTSLKGKE QIKVAHILVK SEKEANDLKN KLNKGADFAK LAGESSLDKA
     SATNGGVIGY ILLNQPGQLV PEFENKAFAL KVNEVSTPVK TDYGWHIIKV LEKKPVPIPT
     KEEAKMTIDN VLAAEILKKY ISDLEAKADL KIMLPPAANN EAKK