ID   MIP_LEGPC               Reviewed;         233 AA.
AC   A5IGB8; P20380; P69059;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
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; OrderedLocusNames=LPC_2500;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7516906; DOI=10.1111/j.1574-6968.1994.tb06798.x;
RA   Ludwig B., Rahfeld J., Schmidt B., Mann K., Wintermeyer E., Fischer G.,
RA   Hacker J.;
RT   "Characterization of Mip proteins of Legionella pneumophila.";
RL   FEMS Microbiol. Lett. 118:23-30(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) 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   -!- SUBCELLULAR LOCATION: Cell outer membrane.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR   EMBL; S72442; AAB31083.1; -; Genomic_DNA.
DR   EMBL; CP000675; ABQ56418.1; -; Genomic_DNA.
DR   RefSeq; WP_011214989.1; NC_009494.2.
DR   AlphaFoldDB; A5IGB8; -.
DR   BMRB; A5IGB8; -.
DR   SMR; A5IGB8; -.
DR   KEGG; lpc:LPC_2500; -.
DR   HOGENOM; CLU_013615_0_1_6; -.
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_0000304998"
FT   DOMAIN          144..233
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
SQ   SEQUENCE   233 AA;  24865 MW;  FE8345428D835323 CRC64;
     MKMKLVTAAV MGLAMSTAMA ATDATSLATD KDKLSYSIGA DLGKNFKNQG IDVNPEAMAK
     GMQDAMSGAQ LALTEQQMKD VLNKFQKDLM AKRTAEFNKK ADENKVKGEA FLTENKNKPG
     VVVLPSGLQY KVINAGNGVK PGKSDTVTVE YTGRLIDGTV FDSTEKTGKP ATFQVSQVIP
     GWTEALQLMP AGSTWEIYVP SGLAYGPRSV GGPIGPNETL IFKIHLISVK KSS