PLP_RICTY
ID PLP_RICTY Reviewed; 282 AA.
AC Q68WG0;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 81.
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=RT0565;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAU04032.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE017197; AAU04032.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_014419445.1; NC_006142.1.
DR AlphaFoldDB; Q68WG0; -.
DR SMR; Q68WG0; -.
DR STRING; 257363.RT0565; -.
DR EnsemblBacteria; AAU04032; AAU04032; RT0565.
DR KEGG; rty:RT0565; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_1_3_5; -.
DR OMA; YEQAKPT; -.
DR OrthoDB; 1838755at2; -.
DR Proteomes; UP000000604; 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 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_0000289287"
FT DOMAIN 138..231
FT /note="PpiC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
SQ SEQUENCE 282 AA; 31596 MW; 26E434297226815D CRC64;
MKKLSVIFLS VSMLSSIAFC DQDKVVATYK GGEVKESQIM QEFKPQLNLQ SGETIKNFDD
FPLQDQEKLI KIYVNNLLLK EEVAKSSITS SKEFQEKLEN AKNQLAQQEL LANYIKSNIT
DKMFDDEYNK YVDNLKGKEQ IKVAHILVKS QKEANTVKTK LSKGGNFNKL AEEFSLDKAT
ASNGGVIGYI ILNQSGQLVP EFENKAFALK VNEVSTPVKT DFGWHIIKVL EKKPVPIPTK
KEAKVTIDNI LAAEILKKYI SDLEAKADLK IMLPKANSKT GS