MIP_LEGPH
ID MIP_LEGPH Reviewed; 233 AA.
AC Q5ZXE0; P20380;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 113.
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=lpg0791;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-40, AND PPIASE
RP ACTIVITY.
RX PubMed=1379319; DOI=10.1111/j.1365-2958.1992.tb00858.x;
RA Fischer G., Bang H., Ludwig B., Mann K., Hacker J.;
RT "Mip protein of Legionella pneumophila exhibits peptidyl-prolyl-cis/trans
RT isomerase (PPlase) activity.";
RL Mol. Microbiol. 6:1375-1383(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 21-233.
RX PubMed=11524681; DOI=10.1038/nsb0901-779;
RA Riboldi-Tunnicliffe A., Konig B., Jessen S., Weiss M.S., Rahfeld J.,
RA Hacker J., Fischer G., Hilgenfeld R.;
RT "Crystal structure of Mip, a prolylisomerase from Legionella pneumophila.";
RL Nat. Struct. Biol. 8:779-783(2001).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAU26880.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; S42595; AAB22717.1; -; Genomic_DNA.
DR EMBL; AE017354; AAU26880.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011213317.1; NC_002942.5.
DR RefSeq; YP_094827.1; NC_002942.5.
DR PDB; 1FD9; X-ray; 2.41 A; A=21-233.
DR PDB; 2UZ5; NMR; -; A=97-233.
DR PDB; 2VCD; NMR; -; A=97-233.
DR PDBsum; 1FD9; -.
DR PDBsum; 2UZ5; -.
DR PDBsum; 2VCD; -.
DR AlphaFoldDB; Q5ZXE0; -.
DR BMRB; Q5ZXE0; -.
DR SMR; Q5ZXE0; -.
DR STRING; 272624.lpg0791; -.
DR PaxDb; Q5ZXE0; -.
DR PRIDE; Q5ZXE0; -.
DR EnsemblBacteria; AAU26880; AAU26880; lpg0791.
DR GeneID; 66489975; -.
DR KEGG; lpn:lpg0791; -.
DR PATRIC; fig|272624.6.peg.819; -.
DR eggNOG; COG0545; Bacteria.
DR HOGENOM; CLU_013615_0_1_6; -.
DR EvolutionaryTrace; Q5ZXE0; -.
DR Proteomes; UP000000609; 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; 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 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Direct protein sequencing; Isomerase;
KW Membrane; Reference proteome; Rotamase; Signal; Virulence.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:1379319"
FT CHAIN 21..233
FT /note="Outer membrane protein MIP"
FT /id="PRO_0000025533"
FT DOMAIN 144..233
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT HELIX 30..49
FT /evidence="ECO:0007829|PDB:1FD9"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:1FD9"
FT HELIX 75..117
FT /evidence="ECO:0007829|PDB:1FD9"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1FD9"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:1FD9"
FT STRAND 146..155
FT /evidence="ECO:0007829|PDB:1FD9"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:1FD9"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:1FD9"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:1FD9"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1FD9"
FT HELIX 180..186
FT /evidence="ECO:0007829|PDB:1FD9"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:1FD9"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1FD9"
FT TURN 204..207
FT /evidence="ECO:0007829|PDB:1FD9"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:1FD9"
FT STRAND 220..230
FT /evidence="ECO:0007829|PDB:1FD9"
SQ SEQUENCE 233 AA; 24881 MW; 6FF95CBCF464CD5A CRC64;
MKMKLVTAAV MGLAMSTAMA ATDATSLATD KDKLSYSIGA DLGKNFKNQG IDVNPEAMAK
GMQDAMSGAQ LALTEQQMKD VLNKFQKDLM AKRTAEFNKK ADENKVKGEA FLTENKNKPG
VVVLPSGLQY KVINSGNGVK PGKSDTVTVE YTGRLIDGTV FDSTEKTGKP ATFQVSQVIP
GWTEALQLMP AGSTWEIYVP SGLAYGPRSV GGPIGPNETL IFKIHLISVK KSS
