ID   MIP_LEGLO               Reviewed;         233 AA.
AC   P53605;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 95.
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   Legionella longbeachae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=450;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33462 / DSM 10572 / NCTC 11477 / Long Beach 4 / Serogroup 1;
RA   Doyle R.M., Manning P.A., Heuzenroeder M.W.;
RL   Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33484 / DSM 25315 / NCTC 11530 / Tucker 1 / Serogroup 2;
RA   Doyle R.M., McLennan A.M., Manning P.A., Heuzenroeder M.W.;
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
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   EMBL; X83036; CAA58145.1; -; Genomic_DNA.
DR   EMBL; AF000958; AAC46211.1; -; Genomic_DNA.
DR   PIR; S57924; S57924.
DR   RefSeq; WP_003636663.1; NZ_CP045308.1.
DR   AlphaFoldDB; P53605; -.
DR   SMR; P53605; -.
DR   OMA; KYMSGHI; -.
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:0000250"
FT   CHAIN           21..233
FT                   /note="Outer membrane protein MIP"
FT                   /id="PRO_0000025531"
FT   DOMAIN          144..233
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ   SEQUENCE   233 AA;  24662 MW;  E0BF1671B9E5B233 CRC64;
     MKMKLVTAAI MGLAMSTAMA ATDATSLTTD KDKLSYSIGA DLGKNFKNQG IDINPDVLAK
     GMQDGMSGAQ LILTEEQMKD VLSKFQKDLM AKRSAEFNKK AEENKAKGDA FLSANKSKPG
     IVVLPSGLQY KIIDAGTGAK PGKSDTVTVE YTGTLIDGTV FDSTEKAGKP ATFQVSQVIP
     GWTEALQLMP AGSTWEVFVP ADLAYGPRSV GGPIGPNETL IFKIHLISVK KAA