Q89A33 (AMIB_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative N-acetylmuramoyl-L-alanine amidase
EC=3.5.1.28

Gene names

Name:	amiB
Ordered Locus Names:	bbp_521

Organism

Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]

Taxonomic identifier

224915 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Baizongia pistaciae)

Protein attributes

Sequence length	217 AA.
Sequence status	Complete.
Protein existence	Inferred 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 process	Cell wall biogenesis/degradation
Cellular component	Secreted
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	peptidoglycan catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	N-acetylmuramoyl-L-alanine amidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 217	217	Putative N-acetylmuramoyl-L-alanine amidase		PRO_0000164423

Sequences

	Sequence		Length	Mass (Da)
	Q89A33 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: F967E3E50F4752A1	FASTA	217	25,202
	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

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.
RefSeq	NP_778118.1. NC_004545.1.
3D structure databases
ProteinModelPortal	Q89A33.
ModBase	Search...
Protein-protein interaction databases
STRING	224915.bbp521.
Proteomic databases
PRIDE	Q89A33.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO27223; AAO27223; bbp_521.
GeneID	1058322.
KEGG	bab:bbp521.
PATRIC	21245863. VBIBucAph80364_0516.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0860.
KO	K01448.
OMA	ASKEFHY.
ProtClustDB	CLSK390915.
Enzyme and pathway databases
BioCyc	BAPH224915:GJ9D-521-MONOMER.
Family and domain databases
Gene3D	3.40.630.40. 2 hits.
InterPro	IPR002508. CW_Hdrlase/autolysin_cat. [Graphical view]
Pfam	PF01520. Amidase_3. 1 hit. [Graphical view]
SMART	SM00646. Ami_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMIB_BUCBP

Accession

Primary (citable) accession number: Q89A33

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program