Protein

Protein accession
Q2I8E6 [UniProt]
Representative
7f6JX
Source
UniProt (cluster: phalp2_17726)
Protein name
N-acetylmuramoyl-L-alanine amidase
Lysin probability
100%
PhaLP type
endolysin
Probability: 99% (predicted by ML model)
Protein sequence
MEIQKKLVDPSKYGTKCPYTMKPKYITVHNTYNDAPAENEVSYMISNNNEVSFHIAVDDKKAIQGIPLERNAWACGDGNGSGNRQSISVEICYSKSGGDRYYKAEDNAVDVVRQLMSMYNIPIENVRTHQSWSGKYCPHRMLAEGRWGAFIQKVKNGNVATTSPTKQNIIQSGAFSPYETPDVMGALTSLKMTADFILQSDGLTYFISKPTSDAQLKAMKEYLDRKGWWYEVK
Physico‐chemical
properties
protein length:233 AA
molecular weight:26267,0 Da
isoelectric point:8,51
hydropathy:-0,59
Representative Protein Details
Accession
7f6JX
Protein name
7f6JX
Sequence length
139 AA
Molecular weight
15761,59530 Da
Isoelectric point
7,69057
Sequence
MEIRKKLVVPSKYGTKCPYTMKPKYITVHNTYNDAPAENEVNYMITNNNEVSFHVAVDDKQAIQGIPWERNAWACGDGNGPGNRESISVEICYSKSGGDRYYKAENNAVDVVRQLMSMYNIPIENVRTHQSWSGKILPT
Other Proteins in cluster: phalp2_17726
Total (incl. this protein): 68 Avg length: 207,8 Avg pI: 6,48

Protein ID Length (AA) pI
7f6JX 139 7,69057
1nWyh 163 7,63572
2dgKy 124 6,80803
31EGE 216 9,10792
3GNrH 209 5,96761
41pyr 102 5,83386
65Pmn 155 7,00560
6oW8g 127 6,89425
6wgFb 120 6,40072
7Xgkt 91 6,03922
7cWWC 224 5,66414
7e37V 196 8,59391
7r0Ku 223 5,51699
7r0LJ 238 8,63910
7r0Nc 172 8,55317
7r1g8 142 6,50581
7vJMi 114 9,51922
7vyfr 161 7,11530
8c9XI 164 6,88754
8s9qN 163 5,94089
Hobu 194 6,21883
A0A2I7SC18 224 5,98022
A0A0C5AMZ6 223 5,51517
A0A2I7SD00 223 5,81801
A0A2I7SCT0 223 5,98824
Similar Clusters (pHMM search)
# Cluster # Members Identity (%) Alignment Length E-value
1 phalp2_13869
7vyfo
1 56,3% 133 1.055E-53
2 phalp2_25038
13C0m
57 50,7% 140 2.481E-52
3 phalp2_12757
86tLk
1 54,2% 118 4.851E-49
4 phalp2_19086
1mxL7
3 54,3% 103 3.172E-41
5 phalp2_29544
3KzTO
225 44,0% 143 4.350E-41
6 phalp2_33479
7swgL
97 45,4% 143 2.634E-39
7 phalp2_18793
1bS71
24 40,7% 140 1.277E-38
8 phalp2_32247
7tHu8
1 56,2% 96 1.652E-34
9 phalp2_8874
2Yvfy
25 39,8% 143 1.369E-32
10 phalp2_29669
8sfID
1005 38,8% 152 6.843E-29

Domains

Domains [InterPro]
Representative sequence (used for alignment): 7f6JX (139 AA)
Member sequence: Q2I8E6 (233 AA)
1 139 AA (representative)
Domain positions follow the representative sequence above; the member sequence bar is scaled to the same axis.
Legend: EAD CBD Linker Disordered Unannotated
Pfam accessions: PF01510

Taxonomy

  Name Taxonomy ID Lineage
Phage Bacillus phage Fah
[NCBI]
345922 Wbetavirus >
Host Bacillus anthracis
[NCBI]
1392 Firmicutes > Bacilli > Bacillales > Bacillaceae > Bacillus > Bacillus cereus group
Host Bacillus cereus
[NCBI]
1396 Firmicutes > Bacilli > Bacillales > Bacillaceae > Bacillus > Bacillus cereus group

Coding sequence (CDS)

Coding sequence (CDS)
CDS Source ID
CDS Source
DQ150593 [NCBI]
CDS location
range 17646 -> 18347
strand +
CDS
ATGGAAATCCAAAAAAAATTAGTTGATCCAAGTAAGTATGGTACAAAGTGTCCGTATACAATGAAGCCTAAATATATCACTGTTCACAACACATATAATGATGCTCCAGCTGAAAATGAAGTGAGTTACATGATTAGTAACAATAATGAGGTGTCGTTTCATATTGCAGTAGATGACAAGAAAGCGATTCAAGGTATTCCGTTGGAACGTAATGCATGGGCTTGCGGAGACGGCAATGGTTCGGGGAATCGTCAATCCATTTCTGTAGAAATCTGTTATTCAAAATCAGGAGGAGATAGATACTATAAAGCTGAGGATAATGCTGTTGATGTTGTACGACAACTTATGTCTATGTACAATATTCCGATTGAAAATGTTCGAACTCATCAATCCTGGTCAGGTAAATATTGTCCGCATAGAATGTTAGCTGAGGGAAGGTGGGGAGCATTCATTCAGAAGGTTAAGAATGGGAATGTGGCGACTACTTCACCAACAAAACAAAACATCATCCAATCAGGGGCTTTCTCACCGTATGAAACCCCTGATGTTATGGGAGCATTAACGTCACTTAAAATGACAGCTGATTTTATCTTACAATCGGATGGATTAACTTATTTTATTTCCAAACCGACTTCAGATGCACAACTAAAAGCAATGAAAGAATACCTTGACCGTAAAGGTTGGTGGTATGAAGTTAAATAA

Gene Ontology

Description Category Evidence (source)
GO:0001897 symbiont-mediated cytolysis of host cell biological process None (UniProt)
GO:0008745 N-acetylmuramoyl-L-alanine amidase activity molecular function None (UniProt)
GO:0009253 peptidoglycan catabolic process biological process None (UniProt)
GO:0009254 peptidoglycan turnover biological process None (UniProt)
GO:0030420 establishment of competence for transformation biological process None (UniProt)
GO:0030435 sporulation resulting in formation of a cellular spore biological process None (UniProt)
GO:0042742 defense response to bacterium biological process None (UniProt)
GO:0071555 cell wall organization biological process None (UniProt)

Enzymatic activity

EC Number Entry Name Reaction Catalyzed Classification Evidence Source
3.5.1.28 None Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. match to sequence model evidence used in automatic assertion
ECO:ECO:0000256
ARBA:ARBA00001561

Tertiary structure

PDB ID
2L47
Method PDB
Resolution –
Chain position –
Model Confidence
Very high
pLDDT > 90
High
90 > pLDDT > 70
Low
70 > pLDDT > 50
Very low
pLDDT < 50
PDB ID
2L48
Method PDB
Resolution –
Chain position –
Model Confidence
Very high
pLDDT > 90
High
90 > pLDDT > 70
Low
70 > pLDDT > 50
Very low
pLDDT < 50
PDB ID
A0A3G8F2L7
Method SMR
Resolution –
Chain position –
Model Confidence
Very high
pLDDT > 90
High
90 > pLDDT > 70
Low
70 > pLDDT > 50
Very low
pLDDT < 50
PDB ID
Q2I8E6
Method SMR
Resolution –
Chain position –
Model Confidence
Very high
pLDDT > 90
High
90 > pLDDT > 70
Low
70 > pLDDT > 50
Very low
pLDDT < 50
PDB ID
Q2LIB5
Method SMR
Resolution –
Chain position –
Model Confidence
Very high
pLDDT > 90
High
90 > pLDDT > 70
Low
70 > pLDDT > 50
Very low
pLDDT < 50

Showing first 5 of 8 structures.


The structures below correspond to the cluster representative (7f6JX) rather than this protein.
PDB ID
7f6JX
Method AlphaFoldv2
Resolution 93.43
Chain position -
Model Confidence
Very high
pLDDT > 90
High
90 > pLDDT > 70
Low
70 > pLDDT > 50
Very low
pLDDT < 50