BARHE:A0A0H3M3F4

Species (Taxon ID)	Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)(Rochalimaea henselae). (283166)
Gene Name(s)	amiB (ECO:0000313 with EMBL:CAF27669.1)
Protein Name(s)	N-acetylmuramoyl-l-alanine amidase (ECO:0000313 with EMBL:CAF27669.1)
External Links
UniProt	A0A0H3M3F4
EMBL	BX897699
RefSeq	WP_011180764.1
PDB	3NE8
PDBsum	3NE8
ProteinModelPortal	A0A0H3M3F4
SMR	A0A0H3M3F4
EnsemblBacteria	CAF27669
GeneID	29620630
KEGG	bhe:BH08710
KO	K01448
OMA	PHRYADF
Proteomes	UP000000421
GO	GO:0016021 GO:0008745 GO:0009253
CDD	cd02696
Gene3D	3.40.630.40
InterPro	IPR002508
Pfam	PF01520
SMART	SM00646

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0008745	N-acetylmuramoyl-L-alanine amidase activity	PMID:22715947	ECO:0000315			F		Figure 1D shows that AmiB mutants have lytic activity. This indicates that these mutants which are increasingly in its active state have increased amidase activity. This increase in unregulated amidase activity results in cell lysis. Figure 2 shows sequence alignment identity and similarities with phage endolysins, lysis enzymes for sporulating bacteria, and lytic enzymes for gram-negative proteobacteria. When compared to phage endolysin there are similar (grey) and identical residues (black) as well as a 50 amino acid section that is not present in phage endolysins that is considered to be used for regulation. The function of this regulation section is described in Figure 3C an alpha helical domain that blocks the substrate from the zinc ion in the active site. Figure 3A and B shows that the core structure of this enzyme is similar to other amidases with exception to the 50 amino acid stretch. Figure S3A (supplemental 3A) shows that three residues that coordinates to the zinc ion in the active site is conserved for LytC-type amidases. Figure 4a shows increased peptidoglycan hydrolase activity for PG sacculi compared to wildtype AmiB when incubated with AmiB mutants that have destabilized regulatory mechanism.	complete CACAO 12912
enables	GO:0008745	N-acetylmuramoyl-L-alanine amidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002508	F		Seeded From UniProt	complete
involved_in	GO:0009253	peptidoglycan catabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002508	P		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000038	ECO:0000323	imported automatically asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
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References

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