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C1A138 (AMPA_RHOE4) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 35. 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:
Probable 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:RER_36150
OrganismRhodococcus erythropolis (strain PR4 / NBRC 100887) [Complete proteome] [HAMAP]
Taxonomic identifier234621 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length505 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 By similarity. 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 By similarity 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
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 – 505505Probable cytosol aminopeptidase HAMAP-Rule MF_00181
PRO_1000203838

Sites

Active site2811 Potential
Active site3551 Potential
Metal binding2691Manganese 2 By similarity
Metal binding2741Manganese 1 By similarity
Metal binding2741Manganese 2 By similarity
Metal binding2921Manganese 2 By similarity
Metal binding3511Manganese 1 By similarity
Metal binding3531Manganese 1 By similarity
Metal binding3531Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
C1A138 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 437D2EFC0C97E40A

FASTA50552,012
        10         20         30         40         50         60 
MSTRTARSLG PDLVLAGTVA KRAEILVVGL TSGPDGPEIA LSEGIVAEDV LAEILDSLIA 

        70         80         90        100        110        120 
VGATGKPEQL TRVPAPSALS VTSVLAVGLG SADKLDSEQI RKSAGAAARS LSGIDTVATT 

       130        140        150        160        170        180 
LSILDLGAAA EGFALGAYSF TEFKSSMTAP GPDSQPLARV ELLVPSPRTK ETKATLARSA 

       190        200        210        220        230        240 
AIAEAVATAR EFVNTPPSHL YPAEFAARAK ALGVEAGLTV QVLDEKALEK GGYGGIIGVG 

       250        260        270        280        290        300 
KGSSRQPRLV RLEYASKKRG ARKVALVGKG ITFDTGGISI KPAAGMENMT SDMGGAAAVI 

       310        320        330        340        350        360 
STVVLAAKLG LPVNVVAYVP MAENMPSATA QRPGDVLTQY GGITIEVVNT DAEGRLILAD 

       370        380        390        400        410        420 
AMVRAGEDNP DYMIDTATLT GAQMVALGNR TPGVMGTDEF RDRVASISQS VGENGWAMPL 

       430        440        450        460        470        480 
PEELRGDLDS KVADMANVTP HRWGGMLVAA HYLKEFVPEG VQWAHIDVAG PAYNTSGPWG 

       490        500 
YTGKGGTGVP VRTMISVLED IAVNG 

« Hide

References

[1]"Comparison of the complete genome sequences of Rhodococcus erythropolis PR4 and Rhodococcus opacus B4."
Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PR4 / NBRC 100887.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008957 Genomic DNA. Translation: BAH34323.1.
RefSeqYP_002767062.1. NC_012490.1.

3D structure databases

ProteinModelPortalC1A138.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING234621.RER_36150.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH34323; BAH34323; RER_36150.
GeneID7715119.
KEGGrer:RER_36150.
PATRIC23193706. VBIRhoEry66701_4131.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0260.
HOGENOMHOG000243129.
KOK01255.
OMARDVANEP.
OrthoDBEOG6FV8B3.
ProtClustDBPRK00913.

Enzyme and pathway databases

BioCycRERY234621:GHDE-3657-MONOMER.

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_RHOE4
AccessionPrimary (citable) accession number: C1A138
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 26, 2009
Last modified: February 19, 2014
This is version 35 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

Peptidase families

Classification of peptidase families and list of entries