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

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera › Buchnera aphidicola › Buchnera aphidicola (Schizaphis graminum)

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	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] [Europe PMC] [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...
Protein-protein interaction databases
STRING	198804.BUsg555.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM68093; AAM68093; BUsg_555.
GeneID	1005636.
KEGG	bas:BUsg555.
PATRIC	21247994. VBIBucAph100086_0588.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0860.
KO	K01448.
OMA	GASIWIT.
ProtClustDB	CLSK390915.
Enzyme and pathway databases
BioCyc	BAPH198804:GHMG-595-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_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:	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