ID   MIP_CHLMU               Reviewed;         243 AA.
AC   Q9PJK1;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   25-MAY-2022, entry version 111.
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=TC_0828;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
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).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF39628.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE002160; AAF39628.1; ALT_INIT; Genomic_DNA.
DR   PIR; D81660; D81660.
DR   RefSeq; WP_010231699.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PJK1; -.
DR   SMR; Q9PJK1; -.
DR   STRING; 243161.TC_0828; -.
DR   EnsemblBacteria; AAF39628; AAF39628; TC_0828.
DR   GeneID; 1246196; -.
DR   KEGG; cmu:TC_0828; -.
DR   eggNOG; COG0545; Bacteria.
DR   HOGENOM; CLU_013615_0_1_0; -.
DR   OrthoDB; 1861282at2; -.
DR   Proteomes; UP000000800; 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.
PE   3: Inferred from homology;
KW   Cell outer membrane; Isomerase; Membrane; Rotamase; Signal.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000255"
FT   CHAIN           15..243
FT                   /note="Peptidyl-prolyl cis-trans isomerase Mip"
FT                   /id="PRO_0000025527"
FT   DOMAIN          152..235
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ   SEQUENCE   243 AA;  26782 MW;  4556004B7511A72C CRC64;
     MKNILSWMLM FAVALPILGC DNNGGSQTSA MGKDMVEDSV LTDNQKLSRT FGHLLARQLS
     STEDFTLDLT EVIKGMQSEI EGKSAPLTDS EYETQMALVQ KASFEKKCSE NLASAEKFLK
     ENKDKEGVIE LEPNKLQYRI VKEGTGRVLT GKPNALLHYT GSFINGKVFD TSEKNKDPIL
     LPLTKVISGF SQGMQGMREG EVRVLYIHPD LAYGTSGQLP PNSLLIFEVK LIEANDDNVS
     VAE