BACSU:XLYA

Species (Taxon ID)	Bacillus subtilis (strain 168). (224308)
Gene Name(s)	xlyA
Protein Name(s)	N-acetylmuramoyl-L-alanine amidase XlyA Autolysin Cell wall hydrolase
External Links
UniProt	P39800
EMBL	Z36941 L25924 Z70177 AL009126 AJ002571
PIR	I39938
RefSeq	NP_389164.1 WP_003245230.1
PDB	3HMB 3RDR
PDBsum	3HMB 3RDR
ProteinModelPortal	P39800
SMR	P39800
STRING	224308.Bsubs1_010100007101
PaxDb	P39800
EnsemblBacteria	CAB13138
GeneID	939869
KEGG	bsu:BSU12810
PATRIC	18974313
eggNOG	ENOG4108VPC COG1388 COG3409 COG5632
HOGENOM	HOG000273688
InParanoid	P39800
KO	K01447
OMA	IYGPATK
PhylomeDB	P39800
BioCyc	BSUB:BSU12810-MONOMER
Proteomes	UP000001570
GO	GO:0005576 GO:0008745 GO:0071555 GO:0030420 GO:0009253 GO:0030435
CDD	cd00118 cd06583
Gene3D	1.10.101.10 3.10.350.10 3.40.80.10
InterPro	IPR002502 IPR018392 IPR002477
Pfam	PF01510 PF01476 PF01471
SMART	SM00644 SM00257
SUPFAM	SSF47090 SSF54106 SSF55846
PROSITE	PS51782

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
Contributes to	GO:0019835	cytolysis	PMID:21816821	ECO:0000250		UniProtKB:Q81WA9	P		In Figure 2, the structures and desirable behaviors were compared between PlyL and XlyA, concluding them to be homologous amidase lysins. Specifically in Panel A of Figure 2, the lysing abilities of the strains were compared on their effect on host cell B. Subtilis. The full-length protein of XlyA was similar to its lysing abilities of the catalytic domain of PlyL, which is responsible for producing amidase, an enzyme that cleaves peptidoglycan in the cell walls of the bacterial host cells.	complete CACAO 12917
involved_in	GO:0009254	peptidoglycan turnover		ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10041 PANTHER:PTN001252273	P		Seeded From UniProt	complete
involved_in	GO:0009253	peptidoglycan catabolic process		ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG13687 PANTHER:PTN001252273	P		Seeded From UniProt	complete
enables	GO:0008745	N-acetylmuramoyl-L-alanine amidase activity		ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG13687 PANTHER:PTN001252273 UniProtKB:G3XCW9 UniProtKB:Q9HT86 UniProtKB:Q9I5D1	F		Seeded From UniProt	complete
enables	GO:0008745	N-acetylmuramoyl-L-alanine amidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002502 InterPro:IPR036505	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:IPR002502 InterPro:IPR036505	P		Seeded From UniProt	complete
enables	GO:0008745	N-acetylmuramoyl-L-alanine amidase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.5.1.28	F		Seeded From UniProt	complete
involved_in	GO:0030435	sporulation resulting in formation of a cellular spore	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0749	P		Seeded From UniProt	complete
involved_in	GO:0030420	establishment of competence for transformation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0178	P		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
involved_in	GO:0071555	cell wall organization	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0961	P		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964 UniProtKB-SubCell:SL-0243	C		Seeded From UniProt	complete
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References

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