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Q5ZXE0 (MIP_LEGPH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Outer membrane protein MIP

EC=5.2.1.8
Alternative name(s):
Macrophage infectivity potentiator
Peptidyl-prolyl cis-trans isomerase
Short name=PPIase
Rotamase
Gene names
Name:mip
Ordered Locus Names:lpg0791
OrganismLegionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) [Complete proteome] [HAMAP]
Taxonomic identifier272624 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length233 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential virulence factor associated with macrophage infectivity. Exhibits PPIase activity.

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulation

Strongly inhibited by FK506 but is completely resistant to cyclosporin A.

Subcellular location

Cell outer membrane.

Sequence similarities

Belongs to the FKBP-type PPIase family.

Contains 1 PPIase FKBP-type domain.

Sequence caution

The sequence AAU26880.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processVirulence
   Cellular componentCell outer membrane
Membrane
   DomainSignal
   Molecular functionIsomerase
Rotamase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

protein folding

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.1
Chain21 – 233213Outer membrane protein MIP
PRO_0000025533

Regions

Domain144 – 23390PPIase FKBP-type

Secondary structure

.............................. 233
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5ZXE0 [UniParc].

Last modified February 1, 2005. Version 2.
Checksum: 6FF95CBCF464CD5A

FASTA23324,881
        10         20         30         40         50         60 
MKMKLVTAAV MGLAMSTAMA ATDATSLATD KDKLSYSIGA DLGKNFKNQG IDVNPEAMAK 

        70         80         90        100        110        120 
GMQDAMSGAQ LALTEQQMKD VLNKFQKDLM AKRTAEFNKK ADENKVKGEA FLTENKNKPG 

       130        140        150        160        170        180 
VVVLPSGLQY KVINSGNGVK PGKSDTVTVE YTGRLIDGTV FDSTEKTGKP ATFQVSQVIP 

       190        200        210        220        230 
GWTEALQLMP AGSTWEIYVP SGLAYGPRSV GGPIGPNETL IFKIHLISVK KSS 

« Hide

References

« Hide 'large scale' references
[1]"Mip protein of Legionella pneumophila exhibits peptidyl-prolyl-cis/trans isomerase (PPlase) activity."
Fischer G., Bang H., Ludwig B., Mann K., Hacker J.
Mol. Microbiol. 6:1375-1383(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-40, PPIASE ACTIVITY.
[2]"The genomic sequence of the accidental pathogen Legionella pneumophila."
Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G., Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V., Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S. expand/collapse author list , Georghiou A., Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A., Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A., Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A., Russo J.J.
Science 305:1966-1968(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Philadelphia 1 / ATCC 33152 / DSM 7513.
[3]"Crystal structure of Mip, a prolylisomerase from Legionella pneumophila."
Riboldi-Tunnicliffe A., Konig B., Jessen S., Weiss M.S., Rahfeld J., Hacker J., Fischer G., Hilgenfeld R.
Nat. Struct. Biol. 8:779-783(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 21-233.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S42595 Genomic DNA. Translation: AAB22717.1.
AE017354 Genomic DNA. Translation: AAU26880.1. Different initiation.
RefSeqYP_007568966.1. NC_020521.1.
YP_094827.1. NC_002942.5.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FD9X-ray2.41A21-233[»]
2UZ5NMR-A97-233[»]
2VCDNMR-A97-233[»]
ProteinModelPortalQ5ZXE0.
SMRQ5ZXE0. Positions 29-232.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272624.lpg0791.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU26880; AAU26880; lpg0791.
GeneID14801115.
3078495.
KEGGlpn:lpg0791.
lpu:LPE509_02423.
PATRIC22328578. VBILegPne29832_0819.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0545.
HOGENOMHOG000154888.
KOK03773.
OrthoDBEOG6DRPKW.

Enzyme and pathway databases

BioCycLPNE272624:GHDI-790-MONOMER.

Family and domain databases

Gene3D1.10.287.460. 1 hit.
InterProIPR008104. INFPOTNTIATR.
IPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
IPR000774. PPIase_FKBP_N.
[Graphical view]
PANTHERPTHR10516. PTHR10516. 1 hit.
PfamPF00254. FKBP_C. 1 hit.
PF01346. FKBP_N. 1 hit.
[Graphical view]
PRINTSPR01730. INFPOTNTIATR.
PROSITEPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ5ZXE0.

Entry information

Entry nameMIP_LEGPH
AccessionPrimary (citable) accession number: Q5ZXE0
Secondary accession number(s): P20380
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: February 1, 2005
Last modified: May 14, 2014
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references