Protein

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Genbank accession
AEJ54375.1 [GenBank]
Protein name
phage-associated cell wall hydrolase
RBP type
TF
Evidence RBPdetect2
Probability 0,70
Seq2Symm
C1 confidence 1,000
C1 1,000
C2 0,010
C3 0,000
Predicted homo-oligomer symmetry (Seq2Symm, per-class probabilities; C1 = monomer, C2 = dimer, C3 = trimer).
Protein sequence
MATDNDIIQFAENLADAGVGTDADGAWGTQCVDLPNSISINFFGRALWGNAIDLLNSAAEAGYEVEYNQVGNLDSRPRRGAVFVMDTTYIAGHPYGHTGLVIEDSDGYTMRTIEQNIDGNADSLYVGGPARYNTRNFDGIVGWFYFPTDNQSQAPAPTLTPFDGIITINEETGTFTVEVSALNVRAGAGLGAEIVAVYGAGETINYDGWCDVDGYIWISYISWSGNRRYVAVGQSENGRRVTSFGSFA
Physico‐chemical
properties
protein length:248 AA
molecular weight: 26737,93890 Da
isoelectric point:4,12551
aromaticity:0,12097
hydropathy:-0,17258

Taxonomy

Phage
Streptococcus phage YMC-2011 [NCBI] · taxon 1051631
Uroviricota Caudoviricetes Aliceevansviridae Streptococcus phage YMC-2011
Host
Streptococcus salivarius 57.I [NCBI] · taxon 1046629
Bacillota Bacilli Lactobacillales Streptococcaceae Streptococcus Streptococcus salivarius

Coding sequence (CDS)

Genbank protein accession
AEJ54375.1 [NCBI]
Genbank nucleotide accession
CP002889 [NCBI]
CDS location
range 5855 -> 6601
strand +
CDS
ATGGCAACAGATAATGACATCATCCAATTTGCGGAAAACCTAGCCGACGCTGGAGTCGGTACCGATGCAGACGGAGCGTGGGGAACGCAATGCGTTGACCTGCCTAACTCTATCTCAATTAACTTCTTTGGCCGCGCTCTTTGGGGCAACGCTATTGACTTGCTCAACTCAGCGGCAGAAGCAGGCTATGAAGTCGAGTATAACCAAGTGGGCAACCTTGACAGTCGTCCACGTCGTGGGGCTGTATTCGTCATGGATACTACTTACATCGCAGGGCACCCATACGGGCACACTGGTCTGGTTATCGAAGATTCGGACGGCTATACCATGCGAACTATCGAGCAGAATATTGACGGTAACGCTGATAGCTTGTATGTTGGTGGCCCCGCTCGTTACAATACACGCAATTTTGACGGCATTGTAGGTTGGTTCTATTTCCCAACAGATAACCAATCCCAAGCCCCTGCACCAACTCTGACCCCGTTTGATGGTATAATTACTATTAACGAGGAAACCGGGACATTCACGGTTGAAGTCTCAGCTCTTAATGTTCGAGCTGGTGCTGGTCTAGGTGCTGAAATTGTGGCAGTCTATGGAGCCGGTGAAACTATCAACTATGATGGTTGGTGTGACGTTGACGGCTATATCTGGATTAGCTACATTAGCTGGTCTGGTAATCGTCGCTATGTTGCAGTCGGTCAATCAGAGAATGGTCGACGTGTCACGTCATTCGGTTCATTCGCTTAA

Genome Context

Tertiary structure

AEJ54375.1
ESMFold2 structure
Source ESMFold2
pLDDT 87.5
Oligomeric state monomer
Download structure