Q8K908 (AMIB_BUCAP) 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:	BUsg_555

Organism

Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]

Taxonomic identifier

198804 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	233 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	cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW 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 – 233	233	Putative N-acetylmuramoyl-L-alanine amidase		PRO_0000164422

Sequences

	Sequence		Length	Mass (Da)
	Q8K908 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 4F492C6C2D5FF31E	FASTA	233	27,259
	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

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]. Strain: Sg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013218 Genomic DNA. Translation: AAM68093.1.
RefSeq	NP_660882.1. NC_004061.1.
3D structure databases
ProteinModelPortal	Q8K908.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBUCT00000000378; EBBUCP00000000378; EBBUCG00000000378.
GeneID	1005636.
GenomeReviews	Gene locus BUsg_555 in contig AE013218_GR.
KEGG	bas:BUsg555.
PATRIC	21247994. VBIBucAph100086_0588.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000007972.
HOGENOM	HBG656726.
OMA	QRENDAD.
ProtClustDB	CLSK390915.
Enzyme and pathway databases
BioCyc	BAPH198804:BUSG555-MONOMER.
Family and domain databases
InterPro	IPR002508. CW_Hdrlase/autolysin_cat. [Graphical view]
Gene3D	G3DSA:3.40.630.40. Cell_wall_OHase/autolysin_cat. 2 hits.
KO	K01448.
Pfam	PF01520. Amidase_3. 1 hit. [Graphical view]
SMART	SM00646. Ami_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMIB_BUCAP

Accession

Primary (citable) accession number: Q8K908

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	October 1, 2002
Last modified:	January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program