P57638 (AMIB_BUCAI) 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:	BU576

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium)

Taxonomic identifier

107806 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	237 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 Reference 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 – 237	237	Putative N-acetylmuramoyl-L-alanine amidase		PRO_0000164421

Sequences

	Sequence		Length	Mass (Da)
	P57638 [UniParc]. Last modified January 11, 2001. Version 1. Checksum: D8FD528FB89C406C	FASTA	237	27,240
	10 20 30 40 50 60 MSKKITILID AGHGGYDPGA IGIRGLKEKN INIEIALKLE KLLNHDKMFC TILTRHNDSY 70 80 90 100 110 120 LSLKKRKQLL KKNQVNFLIS IHADSSRKQN VSGASIWIVS KTRINREINN YLKNKSTLLF 130 140 150 160 170 180 SKKIENIFKQ NKNDFFLKKT ILDLQSNNFQ KIELDLSKEI LKQLEKNTKL NKKYPNYASL 190 200 210 220 230 GILSSINTPS ILIETGFITN ILEGKKLKTT NYQNKIANSI YLGLKNYFTK SSYILKK

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed: 10993077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: APS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000003 Genomic DNA. Translation: BAB13265.1.
RefSeq	NP_240379.1. NC_002528.1.
3D structure databases
ProteinModelPortal	P57638.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBUCT00000003086; EBBUCP00000002862; EBBUCG00000003086.
GeneID	1109915.
GenomeReviews	Gene locus BU576 in contig BA000003_GR.
KEGG	buc:BU576.
PATRIC	21244700. VBIBucAph127364_0580.
Phylogenomic databases
GeneTree	EBGT00050000007972.
HOGENOM	HBG656726.
OMA	GTEVYFY.
PhylomeDB	P57638.
ProtClustDB	CLSK390915.
Enzyme and pathway databases
BioCyc	BSP107806:BU576-MONOMER.
Family and domain databases
InterPro	IPR002508. CW_Hdrlase/autolysin_cat. [Graphical view]
Gene3D	G3DSA:3.40.630.40. Cell_wall_OHase/autolysin_cat. 1 hit.
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_BUCAI

Accession

Primary (citable) accession number: P57638

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	January 11, 2001
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program