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A7GUC8 (AMPA_BACCN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. 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:Bcer98_3532
OrganismBacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]
Taxonomic identifier315749 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length493 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 – 493493Probable cytosol aminopeptidase HAMAP MF_00181
PRO_1000077273

Sites

Active site2711 Potential
Active site3451 Potential
Metal binding2591Manganese 2 By similarity
Metal binding2641Manganese 1 By similarity
Metal binding2641Manganese 2 By similarity
Metal binding2821Manganese 2 By similarity
Metal binding3411Manganese 1 By similarity
Metal binding3431Manganese 1 By similarity
Metal binding3431Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
A7GUC8 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: F876B95C31D750DC

FASTA49353,721
        10         20         30         40         50         60 
MFQVQTELAN HGAVIVALFE EETSRFVQEL DKAFEGQLQG LLDEKELSTK KKSISKVHSL 

        70         80         90        100        110        120 
GKTNVKRYYF VGLGKKEAYT TETLRASLSK TFKTLQAEKI QDAAILLDSF VTEKLDAIDV 

       130        140        150        160        170        180 
AHIAAEVYCL GTYRLQTYKT DKKEHVELEK LVVITAEDAK EIEAALTVGY VHGRATNSAR 

       190        200        210        220        230        240 
TLVNMPPNML TATKLAEYAV ELAEKYDMDY KVLEKEEMEE LGMGALLAVN QGSTEPPKMI 

       250        260        270        280        290        300 
ALIYKGKEEW KDVIGLIGKG ITYDTGGYSL KPRDGMVGMK GDMGGAAAVL GAMEIIGELR 

       310        320        330        340        350        360 
PEQNVIAIIP STDNVVSGTA FKPDDVITSM SGKTIEVLNT DAEGRLALAD GITYAKKLGA 

       370        380        390        400        410        420 
NYLVDVATLT GGVIVALGNH TTGAMTNNET LFEQVLEASM ETDERIWQLP IFERDKERVR 

       430        440        450        460        470        480 
NSKFADLNNS PGRDGHAVMA GTFLGEFAED TPWVHLDIAG TSDTTSTHDL GPAGATGVMV 

       490 
RTLATLVERF GEE 

« 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: NVH 391-98.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000764 Genomic DNA. Translation: ABS23736.1.
RefSeqYP_001376731.1. NC_009674.1.

3D structure databases

ProteinModelPortalA7GUC8.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7GUC8.

Protein family/group databases

MEROPSM17.010.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000036497; EBBACP00000035548; EBBACG00000036488.
GeneID5343661.
GenomeReviewsGene locus Bcer98_3532 in contig CP000764_GR.
KEGGbcy:Bcer98_3532.
PATRIC18935768. VBIBacCyt128034_3700.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0260.
GeneTreeEBGT00050000002613.
HOGENOMHBG742580.
OMACTEEAQL.
ProtClustDBPRK00913.

Enzyme and pathway databases

BioCycBCER315749:BCER98_3532-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_BACCN
AccessionPrimary (citable) accession number: A7GUC8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: September 11, 2007
Last modified: December 14, 2011
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

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families