ID   MIP_TATMI               Reviewed;         243 AA.
AC   P31106;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Outer membrane protein MIP;
DE            EC=5.2.1.8;
DE   AltName: Full=Macrophage infectivity potentiator;
DE   AltName: Full=Peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE   AltName: Full=Rotamase;
DE   Flags: Precursor;
GN   Name=mip;
OS   Tatlockia micdadei (Legionella micdadei).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Tatlockia.
OX   NCBI_TaxID=451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1840577; DOI=10.1128/iai.59.10.3836-3840.1991;
RA   Bangsborg J.M., Cianciotto N.P., Hindersson P.;
RT   "Nucleotide sequence analysis of the Legionella micdadei mip gene, encoding
RT   a 30-kilodalton analog of the Legionella pneumophila Mip protein.";
RL   Infect. Immun. 59:3836-3840(1991).
CC   -!- FUNCTION: Essential virulence factor associated with macrophage
CC       infectivity. Exhibits PPIase activity.
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   -!- ACTIVITY REGULATION: Strongly inhibited by FK506 but is completely
CC       resistant to cyclosporin A.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR   PIR; A43596; A43596.
DR   AlphaFoldDB; P31106; -.
DR   SMR; P31106; -.
DR   STRING; 451.B6N58_05570; -.
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; IPR008104; INFPOTNTIATR.
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   PRINTS; PR01730; INFPOTNTIATR.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Isomerase; Membrane; Rotamase; Signal; Virulence.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..243
FT                   /note="Outer membrane protein MIP"
FT                   /id="PRO_0000025534"
FT   DOMAIN          153..243
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ   SEQUENCE   243 AA;  25930 MW;  E925651B42DC98F4 CRC64;
     MKMRLVAAAA MGLAMSTTIA ATATTDATTS APGTSLTTDT EKLSYSIGAD LGKNFKKQGI
     EISPAAMAKG LQDGMSGGQL LLTDDQMKDV LNKFQKDLMM KRSAEFNKKA EENKSKGEAF
     LNENKSKEGV VSLPSGLQYN ILERGDGAKP TKDDVVTVEY TGKLIDGQVF DSTEKTGKPA
     TFKVSQVIPG WTEALQLMPA GSTWEVYIPS NLAYGPRSVG GPIGPNETLI FKIHLISVKK
     SDA