ID   PLP1_BORBR              Reviewed;         258 AA.
AC   Q7WCX5;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Probable parvulin-type peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase;
DE   Flags: Precursor;
GN   OrderedLocusNames=BB3803;
OS   Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS   (Alcaligenes bronchisepticus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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   -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC       {ECO:0000305}.
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DR   EMBL; BX640448; CAE35777.1; -; Genomic_DNA.
DR   RefSeq; WP_003813874.1; NC_002927.3.
DR   AlphaFoldDB; Q7WCX5; -.
DR   SMR; Q7WCX5; -.
DR   STRING; 257310.BB3803; -.
DR   EnsemblBacteria; CAE35777; CAE35777; BB3803.
DR   GeneID; 56477714; -.
DR   KEGG; bbr:BB3803; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_034646_1_1_4; -.
DR   OMA; YEQAKPT; -.
DR   OrthoDB; 1838755at2; -.
DR   Proteomes; UP000001027; 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   PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE   3: Inferred from homology;
KW   Isomerase; Rotamase; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..258
FT                   /note="Probable parvulin-type peptidyl-prolyl cis-trans
FT                   isomerase"
FT                   /id="PRO_0000312516"
FT   DOMAIN          127..219
FT                   /note="PpiC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
FT   REGION          158..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   258 AA;  28937 MW;  9748CAB763219417 CRC64;
     MKRIAMLAAA CVIAVPAFAQ NVATVNGKPI TQKSLDEFVK LVVSQGATDS PQLREQIKQE
     MINRQVFVQA AEKDGVAKQA DVQTEIELAR QGILVRALMA DYLQKHPVTD AQVKAEYEKI
     KKEQAGKMEY KVRHILVEDE KTANDLLAQV KSNKSKFDDL AKKNSKDPGS AERGGDLGWA
     PATNYVQPFA EAVTKLKKGQ LVDKPVQTQF GWHVIQVDDT RPVEFPAMDQ VRPQLEEMLR
     QQTLANYQKQ LREQAKIQ