PPI1_BRUME
ID PPI1_BRUME Reviewed; 196 AA.
AC Q8YHB5;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 113.
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=BMEI0887;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL52068.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE008917; AAL52068.1; ALT_INIT; Genomic_DNA.
DR PIR; AI3362; AI3362.
DR RefSeq; WP_004683823.1; NZ_GG703780.1.
DR AlphaFoldDB; Q8YHB5; -.
DR SMR; Q8YHB5; -.
DR STRING; 224914.BMEI0887; -.
DR EnsemblBacteria; AAL52068; AAL52068; BMEI0887.
DR GeneID; 45052143; -.
DR KEGG; bme:BMEI0887; -.
DR PATRIC; fig|224914.52.peg.557; -.
DR eggNOG; COG0652; Bacteria.
DR OMA; VPFHRVM; -.
DR PhylomeDB; Q8YHB5; -.
DR Proteomes; UP000000419; 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; 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_0000282595"
FT DOMAIN 29..194
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ SEQUENCE 196 AA; 20751 MW; 5577F02D377FF89B CRC64;
MSFIRSALAA AAFVALSIGA VQTASAADPE NTVILKLKDG DVALELRPDL APKHVAQIKK
LVREGAYNGV AFHRVIPGFM AQTGDVKFGN MDKGFDAARV GTGGSNYPDL PAEFSKEPFV
RGTVGMARSQ NPNSANSQFF IMFDDGPFLN GQYTVVGKVV SGMDAVDKIK KGSEAENGAV
KNPDKIIKAT IEADTK
