Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q8K908 (AMIB_BUCAP)

Last modified January 19, 2010. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Putative N-acetylmuramoyl-L-alanine amidase
    EC=3.5.1.28
Gene names
Name: amiB
Ordered Locus Names: BUsg_555
OrganismBuchnera aphidicola subsp. Schizaphis graminum [Complete proteome] [HAMAP]
Taxonomic identifier98794 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length233 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Cell-wall hydrolase probably involved in cell-wall hydrolysis, septation or recycling 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 processcellular cell wall organization

Inferred from electronic annotation. Source: UniProtKB-KW

peptidoglycan 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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 233233Putative N-acetylmuramoyl-L-alanine amidase
PRO_0000164422

Sequences

Sequence LengthMass (Da)Tools
Q8K908-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 4F492C6C2D5FF31E

FASTA23327,259
        10         20         30         40         50         60 
MIDPGHGGQD PGAINSLGLQ EKKITLKIGI KLKNLLQNSD LFYPVLTRND DSYVSLKKRR 

        70         80         90        100        110        120 
DFLKNNHVSF LISIHADSSK KRYVSGASIW ITTNDRMHRE INNFIKNREE NIYFPKNIQN 

       130        140        150        160        170        180 
LIQKNKHDFF LKKTVLDLQF NNFQKMEINL SRYIFQQLKK IIKLDKINLN YASLGILSSI 

       190        200        210        220        230 
NTPSMLIETG FITNFLEEKK LRTNKYQNKI ANAIYIALKN YFQDRLLSNL RNT 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM68093.1.
RefSeqNP_660882.1.

3D structure databases

SMRQ8K908. Positions 1-225.
ModBaseSearch...

Genome annotation databases

GeneID1005636.
GenomeReviewsGene locus BUsg_555 in contig AE013218_GR.
KEGGbas:BUsg555.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG656726.
OMATHEKDIT.

Enzyme and pathway databases

BioCycBAPH198804:BUSG555-MONOMER.

Family and domain databases

InterProIPR002508. CW_Hdrlase/autolysin_cat.
[Graphical view]
Gene3DG3DSA:3.40.630.40. Cell_wall_OHase/autolysin_cat. 1 hit.
PfamPF01520. Amidase_3. 1 hit.
[Graphical view]
SMARTSM00646. Ami_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMIB_BUCAP
AccessionPrimary (citable) accession number: Q8K908
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: January 19, 2010
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents