ID   MIP_CHLPN               Reviewed;         258 AA.
AC   Q9Z7P3;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 138.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase Mip;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase;
DE   Flags: Precursor;
GN   Name=mip; OrderedLocusNames=CPn_0661, CP_0086, CpB0687;
OS   Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=83558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CWL029;
RX   PubMed=10192388; DOI=10.1038/7716;
RA   Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA   Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT   "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL   Nat. Genet. 21:385-389(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR39;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J138;
RX   PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA   Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA   Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT   "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT   Japan and CWL029 from USA.";
RL   Nucleic Acids Res. 28:2311-2314(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW-183;
RA   Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA   Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT   "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT   other Chlamydia strains based on whole genome sequence analysis.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: PPIases accelerate the folding of proteins.
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}; Peripheral
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR   EMBL; AE001363; AAD18800.1; -; Genomic_DNA.
DR   EMBL; AE002161; AAF37972.1; -; Genomic_DNA.
DR   EMBL; BA000008; BAA98868.1; -; Genomic_DNA.
DR   EMBL; AE009440; AAP98616.1; -; Genomic_DNA.
DR   PIR; B86573; B86573.
DR   PIR; F72052; F72052.
DR   RefSeq; NP_224857.1; NC_000922.1.
DR   RefSeq; WP_010883299.1; NZ_LN847257.1.
DR   AlphaFoldDB; Q9Z7P3; -.
DR   SMR; Q9Z7P3; -.
DR   STRING; 115711.CP_0086; -.
DR   BindingDB; Q9Z7P3; -.
DR   ChEMBL; CHEMBL4105762; -.
DR   EnsemblBacteria; AAD18800; AAD18800; CPn_0661.
DR   EnsemblBacteria; AAF37972; AAF37972; CP_0086.
DR   GeneID; 45050712; -.
DR   KEGG; cpa:CP_0086; -.
DR   KEGG; cpj:mip; -.
DR   KEGG; cpn:CPn_0661; -.
DR   KEGG; cpt:CpB0687; -.
DR   PATRIC; fig|115713.3.peg.731; -.
DR   eggNOG; COG0545; Bacteria.
DR   HOGENOM; CLU_013615_0_1_0; -.
DR   OMA; KYMSGHI; -.
DR   OrthoDB; 1861282at2; -.
DR   Proteomes; UP000000583; Chromosome.
DR   Proteomes; UP000000801; 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   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 1.10.287.460; -; 1.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR000774; PPIase_FKBP_N.
DR   InterPro; IPR036944; PPIase_FKBP_N_sf.
DR   Pfam; PF00254; FKBP_C; 1.
DR   Pfam; PF01346; FKBP_N; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Isomerase; Membrane; Rotamase; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           16..258
FT                   /note="Peptidyl-prolyl cis-trans isomerase Mip"
FT                   /id="PRO_0000025528"
FT   DOMAIN          160..243
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ   SEQUENCE   258 AA;  28330 MW;  65E3CE4EAC022552 CRC64;
     MNRRWNLVLA TVALALSVAS CDVRSKDKDK DQGSLVEYKD NKDTNDIELS DNQKLSRTFG
     HLLARQLRKS EDMFFDIAEV AKGLQAELVC KSAPLTETEY EEKMAEVQKL VFEKKSKENL
     SLAEKFLKEN SKNAGVVEVQ PSKLQYKIIK EGAGKAISGK PSALLHYKGS FINGQVFSSS
     EGNNEPILLP LGQTIPGFAL GMQGMKEGET RVLYIHPDLA YGTAGQLPPN SLLIFEINLI
     QASADEVAAV PQEGNQGE