Protein

UniProt accession

A7J2B5 [UniProt]

Protein name

N-acetylmuramoyl-L-alanine amidase

PhaLP type

endolysin

evidence: GO annotation

probability: 99 % (predicted by ML model)

Protein sequence

MTFLDDIKKGCIKGWLDYKVLPSLTAAQAILESGWGKHAPHNALFGIKADASWTGKSFNTKTQEEYQPGIVTDIVDRFRAYDSWDESILDHGQFLVDNPRYKAVIGETDYKKACHAIKDAGYATASGYAELLIQLIEENDLQEWDREALKNNKEETMTTAKEIVQYCVNLANSGMGVDKDGMYGTQCADLPCFVAKNWFGVDLWGNAIDLLDSASAQGWEVHRMPTEANPRAGATFVMAASGHQFGHTGVVIEDSDGYTMRTVEQNIDGNADALYVGAPARFNTRDFTGVTGWFYPPYQEDAVTQPVSTEPQTSDTIVETPKTGTFTLDVAEINIRRWPSLASEVVGSYKQGDTVNFDSEGYANGYYWISYVGGSGKRNYLAIGQTDKDGNRISLWGKLN

Physico‐chemical properties

protein length:	400 AA
molecular weight:	44232,00000 Da
isoelectric point:	4,73556
aromaticity:	0,11250
hydropathy:	-0,43450

Domains

Domains [InterPro]

IPR002901

14–141

IPR002901 IPR007921 IPR003646

IPR051056

2–162

IPR051056 IPR003646 IPR038765

IPR007921

179–266

IPR007921 IPR002901 IPR003646

Protein sequence: A7J2B5

1 400

Legend: Pfam SMART CDD TIGRFAM HAMAP SUPFAM PRINTS Gene3D PANTHER Other

Domains [InterPro]

InterPro ID	Start	End	Source	Name
IPR002901	14	141	SMART	Mannosyl-glycoprotein endo-beta-N-acetylglucosamidase-like domain
IPR007921	162	295	Pfam	CHAP domain
IPR003646	321	383	Pfam	SH3-like domain, bacterial-type
IPR051056	2	162	PANTHER	Glycosyl Hydrolase Family 73
IPR003646	321	389	Pfam	SH3-like domain, bacterial-type
IPR038765	176	277	SUPFAM	Papain-like cysteine peptidase superfamily
IPR007921	179	266	Pfam	CHAP domain
IPR002901	2	145	SMART	Mannosyl-glycoprotein endo-beta-N-acetylglucosamidase-like domain
IPR003646	321	390	Pfam	SH3-like domain, bacterial-type

Taxonomy

	Name	Taxonomy ID	Lineage
Phage	Streptococcus phage P9 [NCBI]	403905	No lineage information
Host	Streptococcus equi [NCBI]	1336	Bacteria > Firmicutes > Bacilli > Lactobacillales > Streptococcaceae > Streptococcus

Coding sequence (CDS)

Genbank protein accession

ABL61079.1 [NCBI]

Genbank nucleotide accession

DQ864624 [NCBI]

CDS location

range 36356 -> 37558
strand +

CDS

ATGACCTTTTTAGATGATATAAAAAAAGGCTGTATCAAAGGTTGGTTAGATTATAAAGTCTTGCCATCCTTGACAGCTGCTCAAGCAATCTTAGAGAGCGGGTGGGGTAAACATGCCCCCCACAATGCTTTATTTGGTATCAAGGCAGATGCAAGCTGGACTGGCAAGTCATTTAACACTAAAACTCAAGAAGAGTATCAGCCTGGTATCGTCACGGATATTGTAGACCGCTTTAGGGCTTACGATAGTTGGGATGAGTCAATTCTTGATCACGGACAATTTTTAGTCGATAATCCACGCTACAAAGCTGTGATTGGAGAGACTGACTATAAAAAAGCCTGTCATGCTATAAAAGATGCAGGCTATGCGACAGCTAGCGGCTATGCGGAACTGCTTATCCAGTTGATTGAGGAAAACGACCTACAAGAATGGGATAGGGAAGCTCTTAAAAATAATAAGGAGGAAACGATGACGACCGCAAAGGAAATTGTACAATACTGTGTTAACCTCGCAAACTCTGGGATGGGAGTTGATAAAGATGGTATGTATGGCACGCAATGCGCTGACTTGCCATGTTTTGTCGCTAAAAATTGGTTCGGAGTCGATTTATGGGGTAACGCGATTGATTTATTAGACAGCGCAAGTGCTCAAGGTTGGGAAGTCCATCGTATGCCAACAGAGGCAAATCCACGAGCGGGGGCTACGTTTGTAATGGCTGCTTCTGGGCATCAATTTGGGCACACAGGAGTTGTCATTGAGGATAGCGACGGTTATACCATGCGTACTGTTGAGCAAAACATTGATGGCAATGCAGACGCTCTGTACGTTGGCGCACCAGCTCGTTTTAATACTCGTGACTTTACTGGTGTGACGGGTTGGTTTTACCCACCATATCAAGAAGATGCCGTTACACAACCAGTCAGCACCGAGCCGCAAACGTCTGACACCATCGTAGAGACTCCAAAAACAGGTACTTTTACGCTAGATGTTGCAGAGATTAACATTAGACGTTGGCCAAGTCTCGCCAGCGAAGTAGTAGGCAGCTATAAGCAAGGTGACACCGTTAACTTTGACAGCGAGGGCTACGCTAATGGCTACTACTGGATTAGCTATGTCGGTGGCTCTGGTAAGCGTAATTACCTAGCGATTGGACAGACTGATAAAGATGGAAACCGTATCAGCCTTTGGGGGAAATTAAATTAG

Gene Ontology

	Description	Category	Evidence (source)
GO:0001897	symbiont-mediated cytolysis of host cell	Biological process	Inferred from Electronic Annotation (InterPro)
GO:0004040	amidase activity	Molecular function	Inferred from Electronic Annotation (UniProt)

Enzymatic activity

EC Number	Entry Name	Reaction Catalyzed	Classification	Evidence	Source
3.5.1.28	N-acetylmuramoyl-L-alanine amidase	residues in certain cell-wall glycopeptides	Hydrolases Acting on carbon-nitrogen bonds, other than peptide bonds In linear amides	match to sequence model evidence used in automatic assertion ECO:0000256	ARBA:ARBA00001561

Tertiary structure

No tertiary structures available.