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A9VMY8 (AMPA_BACWK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. 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:BcerKBAB4_4743
OrganismBacillus weihenstephanensis (strain KBAB4) [Complete proteome] [HAMAP]
Taxonomic identifier315730 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length494 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 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 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 MF_00181

Subcellular location

Cytoplasm By similarity HAMAP 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-KW

manganese ion binding

Inferred from electronic annotation. Source: InterPro

metalloexopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494Probable cytosol aminopeptidase HAMAP MF_00181
PRO_1000098304

Sites

Active site2721 Potential
Active site3461 Potential
Metal binding2601Manganese 2 By similarity
Metal binding2651Manganese 1 By similarity
Metal binding2651Manganese 2 By similarity
Metal binding2831Manganese 2 By similarity
Metal binding3421Manganese 1 By similarity
Metal binding3441Manganese 1 By similarity
Metal binding3441Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
A9VMY8 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 94D55C76BD29A329

FASTA49453,545
        10         20         30         40         50         60 
MFRVQKELVS HEAVIVALFE EDKKSSFVQE LDKAFEGQLQ VLLEEKELST KKKAISKVHS 

        70         80         90        100        110        120 
LGKTNVKRYY FVGLGKKESY TTETLRAALG KAFKALQAAK VQDAAILLDS FVTDKLDAID 

       130        140        150        160        170        180 
VAHIAAEVQG LGTYELQTYK ADKKDRVELE KFTAITAEDA QEIEAALTVG YVHGRATNSA 

       190        200        210        220        230        240 
RTLVNMPPNV LTATKLAEYA VELAEKYDMD YKVLEKEEME ELGMGALLAV NQGSTEPPKM 

       250        260        270        280        290        300 
IALIYKGKEE WKDVIGFVGK GITYDTGGYS LKPREGMVGM KGDMGGAAAV LGAMEIIGEL 

       310        320        330        340        350        360 
RPEQNVIAVI PSTDNVVSGT AFKPDDVITS MSGKTIEVLN TDAEGRLALA DGITYAKKLG 

       370        380        390        400        410        420 
ANYLVDVATL TGGVIVALGN HTTGAMTNNE ELFEQVLEAS METDEPIWQL PIFERDKERV 

       430        440        450        460        470        480 
KNSKFADLNN SPGREGHAVM AGTFIGEFAE ETPWVHLDIA GTSETSGAHD LGPSGATGAM 

       490 
VRTLATLVER FGEE 

« Hide

References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KBAB4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000903 Genomic DNA. Translation: ABY45893.1.
RefSeqYP_001647521.1. NC_010184.1.

3D structure databases

ProteinModelPortalA9VMY8.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9VMY8.

Protein family/group databases

MEROPSM17.010.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000077462; EBBACP00000075396; EBBACG00000077453.
GeneID5844983.
GenomeReviewsGene locus BcerKBAB4_4743 in contig CP000903_GR.
KEGGbwe:BcerKBAB4_4743.
PATRIC19014221. VBIBacWei55973_5398.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000002613.
HOGENOMHBG742580.
OMAFMINLAT.
ProtClustDBPRK00913.

Enzyme and pathway databases

BioCycBWEI315730:BCERKBAB4_4743-MONOMER.

Family and domain databases

HAMAPMF_00181. Cytosol_peptidase_M17.
[Tree]
InterProIPR011356. Peptidase_M17.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_cytosol_amino.
IPR008283. Peptidase_M17_N.
[Graphical view]
KOK01255.
PANTHERPTHR11963:SF3. Peptidase_M17. 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_BACWK
AccessionPrimary (citable) accession number: A9VMY8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: January 25, 2012
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families