Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P27888 (AMPA_RICPR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Cytosol aminopeptidase

EC=3.4.11.1
Alternative name(s):
Leucine aminopeptidase
Short name=LAP
EC=3.4.11.10
Leucyl aminopeptidase
Gene names
Name:pepA
Ordered Locus Names:RP142
OrganismRickettsia prowazekii (strain Madrid E) [Reference proteome] [HAMAP]
Taxonomic identifier272947 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. HAMAP-Rule MF_00181

Catalytic activity

Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. HAMAP-Rule MF_00181

Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.

Cofactor

Binds 2 manganese ions per subunit By similarity. HAMAP-Rule MF_00181

Subcellular location

Cytoplasm HAMAP-Rule MF_00181.

Sequence similarities

Belongs to the peptidase M17 family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandManganese
Metal-binding
   Molecular functionAminopeptidase
Hydrolase
Protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metalloexopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 500500Cytosol aminopeptidase HAMAP-Rule MF_00181
PRO_0000165792

Sites

Active site2771 Potential
Active site3511 Potential
Metal binding2651Manganese 2 By similarity
Metal binding2701Manganese 1 By similarity
Metal binding2701Manganese 2 By similarity
Metal binding2881Manganese 2 By similarity
Metal binding3471Manganese 1 By similarity
Metal binding3491Manganese 1 By similarity
Metal binding3491Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P27888 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: E87FFDEA47EC7C83

FASTA50054,006
        10         20         30         40         50         60 
MLNINFVNEE SSTNQGLIVF IDEQLKLNNN LIALDQQHYE LISKTIQNKL QFSGNYGQIT 

        70         80         90        100        110        120 
VVPSVIKSCA VKYLIIVGLG NVEKLTEAKI EELGGKILQH ATCAKIATIG LKIINRINRF 

       130        140        150        160        170        180 
TSPTFTSLIA SGAFLASYRF HKYKTTLKEV EKFAVESIEI LTDNNSEAMK LFEVKKLIAE 

       190        200        210        220        230        240 
AVFFTRDISN EPSNIKTPQV YAERIVEILE PLGVNIDVIG EHDIKNLGMG ALLGVGQGSQ 

       250        260        270        280        290        300 
NESKLVVMEY KGGSRDDSTL ALVGKGVIFD TGGISLKPSS NMHLMRYDMA GSAAVVGTII 

       310        320        330        340        350        360 
ALASQKVPVN VVGVVGLVEN MQSGNAQRPG DVVVTMSGQT AEVLNTDAEG RLVLADTVWY 

       370        380        390        400        410        420 
VQEKFNPKCV IDVATLTGAI TVALGSTYAG CFSNNDELAD KLIKAGEAVN EKLWRMPLHD 

       430        440        450        460        470        480 
DYDAMINSDI ADIANIGNVP GAAGSCTAAH FIKRFIKDGV DWAHLDIAGV ANSNNASALC 

       490        500 
PKGAVGYGVR LLEKFIKEYN 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the Rickettsia prowazekii pepA gene encoding leucine aminopeptidase."
Wood D.O., Solomon M.J., Speed R.R.
J. Bacteriol. 175:159-165(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Madrid E.
[2]"The genome sequence of Rickettsia prowazekii and the origin of mitochondria."
Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G.
Nature 396:133-140(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Madrid E.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M68966 Genomic DNA. Translation: AAA26388.1.
AJ235270 Genomic DNA. Translation: CAA14610.1.
PIRA40631.
RefSeqNP_220533.1. NC_000963.1.

3D structure databases

ProteinModelPortalP27888.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272947.RP142.

Protein family/group databases

MEROPSM17.003.

Proteomic databases

PRIDEP27888.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAA14610; CAA14610; CAA14610.
GeneID883797.
KEGGrpr:RP142.
PATRIC17901028. VBIRicPro72556_0145.

Phylogenomic databases

eggNOGCOG0260.
HOGENOMHOG000243129.
KOK01255.
OMADMKYDMA.
OrthoDBEOG6FV8B3.
ProtClustDBPRK00913.

Family and domain databases

HAMAPMF_00181. Cytosol_peptidase_M17.
InterProIPR011356. Leucine_aapep/pepB.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_leu_NH2_pept.
IPR008283. Peptidase_M17_N.
[Graphical view]
PANTHERPTHR11963:SF3. PTHR11963:SF3. 1 hit.
PfamPF00883. Peptidase_M17. 1 hit.
PF02789. Peptidase_M17_N. 1 hit.
[Graphical view]
PRINTSPR00481. LAMNOPPTDASE.
PROSITEPS00631. CYTOSOL_AP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPA_RICPR
AccessionPrimary (citable) accession number: P27888
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: February 19, 2014
This is version 96 of the entry and version 1 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

Rickettsia prowazekii

Rickettsia prowazekii (strain Madrid E): entries and gene names

Peptidase families

Classification of peptidase families and list of entries