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Q89A33 (AMIB_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Putative N-acetylmuramoyl-L-alanine amidase

EC=3.5.1.28
Gene names
Name:amiB
Ordered Locus Names:bbp_521
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length217 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Cell-wall hydrolase involved in septum cleavage during cell division By similarity.

Catalytic activity

Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.

Subcellular location

Secreted Potential.

Sequence similarities

Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentSecreted
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpeptidoglycan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionN-acetylmuramoyl-L-alanine amidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 217217Putative N-acetylmuramoyl-L-alanine amidase
PRO_0000164423

Sequences

Sequence LengthMass (Da)Tools
Q89A33 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: F967E3E50F4752A1

FASTA21725,202
        10         20         30         40         50         60 
MIIAIDAGHG GQDPGAIGKN KFQEKNITLS IAKKLTKLLN HTNFFKAVMI RRGNYFLSVF 

        70         80         90        100        110        120 
KRTQIAEKYH ANLLISIHAN SSKNRKISGV SIWVLPKNVH NTRIQKHKLN KKTKNIHKKI 

       130        140        150        160        170        180 
NTKTSKFKNF YEIEYDLAKI IIQELRKVST LNQKKPKYAK FGILKFSQFP SILVETGFIS 

       190        200        210 
NPIEEQHLNK KFYQNLISKS ISIALKKYFL KRIKQYN 

« Hide

References

[1]"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016826 Genomic DNA. Translation: AAO27223.1.
RefSeqNP_778118.1. NC_004545.1.

3D structure databases

ProteinModelPortalQ89A33.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224915.bbp521.

Proteomic databases

PRIDEQ89A33.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO27223; AAO27223; bbp_521.
GeneID1058322.
KEGGbab:bbp521.
PATRIC21245863. VBIBucAph80364_0516.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0860.
KOK01448.
OMAFMSNRMD.
OrthoDBEOG6CP3X3.
ProtClustDBCLSK390915.

Enzyme and pathway databases

BioCycBAPH224915:GJ9D-521-MONOMER.

Family and domain databases

Gene3D3.40.630.40. 2 hits.
InterProIPR002508. CW_Hdrlase/autolysin_cat.
[Graphical view]
PfamPF01520. Amidase_3. 1 hit.
[Graphical view]
SMARTSM00646. Ami_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMIB_BUCBP
AccessionPrimary (citable) accession number: Q89A33
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 2003
Last modified: November 13, 2013
This is version 63 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