PPI1_BRUA2
ID PPI1_BRUA2 Reviewed; 196 AA.
AC Q2YPY5;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Probable peptidyl-prolyl cis-trans isomerase;
DE Short=PPIase;
DE EC=5.2.1.8;
DE AltName: Full=Rotamase;
DE Flags: Precursor;
GN Name=ppi; OrderedLocusNames=BAB1_1118;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
CC -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC cis-trans isomerization of proline imidic peptide bonds in
CC oligopeptides (By similarity). {ECO:0000250}.
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: Periplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC {ECO:0000305}.
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DR EMBL; AM040264; CAJ11074.1; -; Genomic_DNA.
DR RefSeq; WP_002964222.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YPY5; -.
DR SMR; Q2YPY5; -.
DR STRING; 359391.BAB1_1118; -.
DR PRIDE; Q2YPY5; -.
DR EnsemblBacteria; CAJ11074; CAJ11074; BAB1_1118.
DR GeneID; 3787768; -.
DR KEGG; bmf:BAB1_1118; -.
DR PATRIC; fig|359391.11.peg.19; -.
DR HOGENOM; CLU_012062_16_6_5; -.
DR OMA; VPFHRVM; -.
DR PhylomeDB; Q2YPY5; -.
DR Proteomes; UP000002719; Chromosome I.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR024936; Cyclophilin-type_PPIase.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR044666; Cyclophilin_A-like.
DR PANTHER; PTHR45625; PTHR45625; 1.
DR Pfam; PF00160; Pro_isomerase; 1.
DR PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SUPFAM; SSF50891; SSF50891; 1.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Isomerase; Periplasm; Reference proteome; Rotamase; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..196
FT /note="Probable peptidyl-prolyl cis-trans isomerase"
FT /id="PRO_0000282594"
FT DOMAIN 29..194
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 196 AA; 20751 MW; D557A52D322FAE7D CRC64;
MSFIRSALAA AAFVALSIGA VQTASAADPE NTVILKLKDG DVALEIRPDL APKHVAQIKK
LVREGAYNGV AFHRVIPGFM AQTGDVKFGN MDKGFDAARV GTGGSNYPDL PAEFSKEPFV
RGTVGMARSQ NPNSANSQFF IMFDDGPFLN GQYTVVGKVV SGMDAVDKIK KGSEAENGAV
KNPDKIIKAT IEADTK