ID   MIP_CHLTR               Reviewed;         243 AA.
AC   P26623;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 3.
DT   25-MAY-2022, entry version 131.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase Mip;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=27 kDa membrane protein;
DE   AltName: Full=Chl-Mip;
DE   AltName: Full=Rotamase;
DE   Flags: Precursor;
GN   Name=mip; OrderedLocusNames=CT_541;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=L2, Serovar B, and Serovar E;
RX   PubMed=1406289; DOI=10.1111/j.1365-2958.1992.tb01430.x;
RA   Lundemose A.G., Rouch D.A., Birkelund S., Christiansen G., Pearce J.H.;
RT   "Chlamydia trachomatis Mip-like protein.";
RL   Mol. Microbiol. 6:2539-2548(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 69-243.
RC   STRAIN=L2;
RX   PubMed=2013997; DOI=10.1111/j.1365-2958.1991.tb01831.x;
RA   Lundemose A.G., Birkelund S., Fey S.J., Mose Larsen P., Christiansen G.;
RT   "Chlamydia trachomatis contains a protein similar to the Legionella
RT   pneumophila mip gene product.";
RL   Mol. Microbiol. 5:109-115(1991).
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.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR   EMBL; X66126; CAA46917.1; -; Genomic_DNA.
DR   EMBL; X66127; CAA46918.1; -; Genomic_DNA.
DR   EMBL; X66128; CAA46919.1; -; Genomic_DNA.
DR   EMBL; AE001273; AAC68143.1; -; Genomic_DNA.
DR   PIR; S25255; S25255.
DR   PIR; S28638; S28638.
DR   RefSeq; NP_220056.1; NC_000117.1.
DR   RefSeq; WP_009871905.1; NC_000117.1.
DR   AlphaFoldDB; P26623; -.
DR   SMR; P26623; -.
DR   STRING; 813.O172_02975; -.
DR   EnsemblBacteria; AAC68143; AAC68143; CT_541.
DR   GeneID; 884327; -.
DR   KEGG; ctr:CT_541; -.
DR   PATRIC; fig|272561.5.peg.586; -.
DR   HOGENOM; CLU_013615_0_1_0; -.
DR   InParanoid; P26623; -.
DR   OMA; KYMSGHI; -.
DR   Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR   Reactome; R-HSA-166058; MyD88:MAL(TIRAP) cascade initiated on plasma membrane.
DR   Reactome; R-HSA-168188; Toll Like Receptor TLR6:TLR2 Cascade.
DR   Reactome; R-HSA-5602498; MyD88 deficiency (TLR2/4).
DR   Reactome; R-HSA-5603041; IRAK4 deficiency (TLR2/4).
DR   Proteomes; UP000000431; 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; Reference proteome; Rotamase;
KW   Signal.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000255"
FT   CHAIN           15..243
FT                   /note="Peptidyl-prolyl cis-trans isomerase Mip"
FT                   /id="PRO_0000025529"
FT   DOMAIN          152..235
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   VARIANT         56
FT                   /note="S -> A (in strain: L2)"
FT   VARIANT         117
FT                   /note="K -> E (in strain: L2)"
FT   CONFLICT        137..138
FT                   /note="QY -> HD (in Ref. 3)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   243 AA;  26663 MW;  677F9D551A95A382 CRC64;
     MKNILSWMLM FAVALPIVGC DNGGGSQTSA TEKSMVEDSA LTDNQKLSRT FGHLLSRQLS
     RTEDFSLDLV EVIKGMQSEI DGQSAPLTDT EYEKQMAEVQ KASFEAKCSE NLASAEKFLK
     ENKEKAGVIE LEPNKLQYRV VKEGTGRVLS GKPTALLHYT GSFIDGKVFD SSEKNKEPIL
     LPLTKVIPGF SQGMQGMKEG EVRVLYIHPD LAYGTAGQLP PNSLLIFEVK LIEANDDNVS
     VTE