ID   D0J2H9_COMT2            Unreviewed;       175 AA.
AC   D0J2H9; A0A0M2LHV6; D8DD45;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   29-SEP-2021, entry version 66.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363019};
DE            Short=PPIase {ECO:0000256|RuleBase:RU363019};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU363019};
GN   OrderedLocusNames=CtCNB1_1199 {ECO:0000313|EMBL:ACY31945.1};
OS   Comamonas testosteroni (strain CNB-2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=688245 {ECO:0000313|EMBL:ACY31945.1, ECO:0000313|Proteomes:UP000002360};
RN   [1] {ECO:0000313|EMBL:ACY31945.1, ECO:0000313|Proteomes:UP000002360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNB-2 {ECO:0000313|Proteomes:UP000002360};
RX   PubMed=19734336; DOI=10.1128/AEM.00933-09;
RA   Ma Y.F., Zhang Y., Zhang J.Y., Chen D.W., Zhu Y., Zheng H., Wang S.Y.,
RA   Jiang C.Y., Zhao G.P., Liu S.J.;
RT   "The complete genome of Comamonas testosteroni reveals its genetic
RT   adaptations to changing environments.";
RL   Appl. Environ. Microbiol. 75:6812-6819(2009).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. {ECO:0000256|RuleBase:RU363019}.
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         Evidence={ECO:0000256|ARBA:ARBA00000971,
CC         ECO:0000256|RuleBase:RU363019};
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000256|ARBA:ARBA00007365, ECO:0000256|RuleBase:RU363019}.
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DR   EMBL; CP001220; ACY31945.1; -; Genomic_DNA.
DR   STRING; 688245.CtCNB1_1199; -.
DR   EnsemblBacteria; ACY31945; ACY31945; CtCNB1_1199.
DR   KEGG; ctt:CtCNB1_1199; -.
DR   eggNOG; COG0652; Bacteria.
DR   HOGENOM; CLU_012062_16_9_4; -.
DR   OMA; RASIQNE; -.
DR   OrthoDB; 1861282at2; -.
DR   Proteomes; UP000002360; Chromosome.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; 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; IPR044665; E_coli_cyclophilin_A-like.
DR   PANTHER; PTHR43246; PTHR43246; 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 {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU363019};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002360};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU363019}.
FT   DOMAIN          21..174
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
SQ   SEQUENCE   175 AA;  19062 MW;  5F533E9336EF2AAD CRC64;
     MSNPQVELHV TINVADTATQ GVITLELDAV NAPKSTENFL NYVNQGFYNG TIFHRVIKNF
     MIQGGGFAAD MKQKDTAAPI ENEAKNGLKN DKYTIAMART SDPHSATAQF FINTVDNGFL
     NHTAPTGQGW GYAVFGKVVK GEEVVDAIKK VRTTRKGFHD DVPFDAVVID KAVAL
//