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Conserved domains on  [gi|15830876|ref|NP_309649|]
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phage endolysin [Escherichia coli O157:H7 str. Sakai]

Protein Classification

glycoside hydrolase family 104 protein( domain architecture ID 10008704)

glycoside hydrolase family 104 protein similar to Escherichia virus P2 endolysin (also called lysozyme) with transglycosylase activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to programmed host cell lysis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4678 COG4678
Muramidase (phage lambda lysozyme) [Cell wall/membrane/envelope biogenesis, Mobilome: ...
 1-151 2.04e-80

Muramidase (phage lambda lysozyme) [Cell wall/membrane/envelope biogenesis, Mobilome: prophages, transposons];


:

Pssm-ID: 443714  Cd Length: 166  Bit Score: 234.81  E-value: 2.04e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830876   1 MQNLNPQRKAFLDMLAWSEGTDNGRQPtrnhgYDVIVGGELFTDYSDHPRKLVTL---HPKLKSTAAGRYQLLSRWWDAY 77
Cdd:COG4678  13 MSGGDPNVRAFLRTIAASEGTDGSDDG-----YRVLYGGGLFSDLSDHPRICVTIvipNKGNCSTAAGRYQFLNTTWDEY 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830876  78 RKQLGLKDFSPKSQDAVALQQIKERGALPMIDRGDIRQAIDRCSNIWASLPGAGYGQFEHKADSLIAKFKEAGG 151
Cdd:COG4678  88 AKKLGLPDFSPESQDRVALQLLRDRGALELIRAGRIEEALKKLSGTWASLPGAGYGQEENSTDKLPAIYQKALG 161
 
Name Accession Description Interval E-value
COG4678 COG4678
Muramidase (phage lambda lysozyme) [Cell wall/membrane/envelope biogenesis, Mobilome: ...
 1-151 2.04e-80

Muramidase (phage lambda lysozyme) [Cell wall/membrane/envelope biogenesis, Mobilome: prophages, transposons];


Pssm-ID: 443714  Cd Length: 166  Bit Score: 234.81  E-value: 2.04e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830876   1 MQNLNPQRKAFLDMLAWSEGTDNGRQPtrnhgYDVIVGGELFTDYSDHPRKLVTL---HPKLKSTAAGRYQLLSRWWDAY 77
Cdd:COG4678  13 MSGGDPNVRAFLRTIAASEGTDGSDDG-----YRVLYGGGLFSDLSDHPRICVTIvipNKGNCSTAAGRYQFLNTTWDEY 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830876  78 RKQLGLKDFSPKSQDAVALQQIKERGALPMIDRGDIRQAIDRCSNIWASLPGAGYGQFEHKADSLIAKFKEAGG 151
Cdd:COG4678  88 AKKLGLPDFSPESQDRVALQLLRDRGALELIRAGRIEEALKKLSGTWASLPGAGYGQEENSTDKLPAIYQKALG 161
lambda_lys-like cd00736
Bacteriophage lambda lysozyme and similar proteins; Lysozyme from bacteriophage lambda ...
 6-151 5.78e-80

Bacteriophage lambda lysozyme and similar proteins; Lysozyme from bacteriophage lambda hydrolyzes the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), as do other lysozymes. However, unlike other lysozymes, bacteriophage lambda does not produce a reducing end upon cleavage of the peptidoglycan, but rather uses the 6-OH of the same MurNAc residue to produce a 1,6-anhydromuramic acid terminal residue and is therefore a lytic transglycosylase. An identical 1,6-anhydro bond is formed in bacterial peptidoglycans by the action of the lytic transglycosylases of E. coli, though they differ structurally.


Pssm-ID: 381598  Cd Length: 141  Bit Score: 232.82  E-value: 5.78e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830876   6 PQRKAFLDMLAWSEGTdngrqpTRNHGYDVIVGGELFTDYSDHPRKLVTL-HPKLKSTAAGRYQLLSRWWDAYRKQLGLK 84
Cdd:cd00736   1 PNVRAFLDMIAVAEGT------SGDDGYRVLFGGGLFSDFSDHPRILVCRkGGGLKSTAAGAYQFLGRTWDDLAKQLGLP 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830876  85 DFSPKSQDAVALQQIKERGALPMIDRGDIRQAIDRCSNIWASLPGAGYGQFEHKADSLIAKFKEAGG 151
Cdd:cd00736  75 DFSPESQDLAAIALIKERGALDDILAGRIEEAIAKLAKEWASLPGSGYGQPEHSMEELLAKYEKALG 141
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 33-140 2.17e-28

Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 100.89  E-value: 2.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830876    33 YDVIVGGELFTDYSDHPRKLvtlhpklKSTAAGRYQLLSRWWDAYRKQLGL-KDFSPKSQDAVALQQIKE----RGALPM 107
Cdd:pfam00959   1 YWTIGIGHNGKDVSPHPRAT-------KSEAAGRLQIDLDTAERCINQYHKvKDFNPNQQDALVSLAFNVgcgkRGFSTL 73

                          90       100       110
                  ....*....|....*....|....*....|....
gi 15830876   108 IDRGDIRQAIDRCSNIWASLP-GAGYGQFEHKAD 140
Cdd:pfam00959  74 LRAGNIGQWIKACSAIWKSLKaGKVYNGLVNRRE 107
 
Name Accession Description Interval E-value
COG4678 COG4678
Muramidase (phage lambda lysozyme) [Cell wall/membrane/envelope biogenesis, Mobilome: ...
 1-151 2.04e-80

Muramidase (phage lambda lysozyme) [Cell wall/membrane/envelope biogenesis, Mobilome: prophages, transposons];


Pssm-ID: 443714  Cd Length: 166  Bit Score: 234.81  E-value: 2.04e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830876   1 MQNLNPQRKAFLDMLAWSEGTDNGRQPtrnhgYDVIVGGELFTDYSDHPRKLVTL---HPKLKSTAAGRYQLLSRWWDAY 77
Cdd:COG4678  13 MSGGDPNVRAFLRTIAASEGTDGSDDG-----YRVLYGGGLFSDLSDHPRICVTIvipNKGNCSTAAGRYQFLNTTWDEY 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830876  78 RKQLGLKDFSPKSQDAVALQQIKERGALPMIDRGDIRQAIDRCSNIWASLPGAGYGQFEHKADSLIAKFKEAGG 151
Cdd:COG4678  88 AKKLGLPDFSPESQDRVALQLLRDRGALELIRAGRIEEALKKLSGTWASLPGAGYGQEENSTDKLPAIYQKALG 161
lambda_lys-like cd00736
Bacteriophage lambda lysozyme and similar proteins; Lysozyme from bacteriophage lambda ...
 6-151 5.78e-80

Bacteriophage lambda lysozyme and similar proteins; Lysozyme from bacteriophage lambda hydrolyzes the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), as do other lysozymes. However, unlike other lysozymes, bacteriophage lambda does not produce a reducing end upon cleavage of the peptidoglycan, but rather uses the 6-OH of the same MurNAc residue to produce a 1,6-anhydromuramic acid terminal residue and is therefore a lytic transglycosylase. An identical 1,6-anhydro bond is formed in bacterial peptidoglycans by the action of the lytic transglycosylases of E. coli, though they differ structurally.


Pssm-ID: 381598  Cd Length: 141  Bit Score: 232.82  E-value: 5.78e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830876   6 PQRKAFLDMLAWSEGTdngrqpTRNHGYDVIVGGELFTDYSDHPRKLVTL-HPKLKSTAAGRYQLLSRWWDAYRKQLGLK 84
Cdd:cd00736   1 PNVRAFLDMIAVAEGT------SGDDGYRVLFGGGLFSDFSDHPRILVCRkGGGLKSTAAGAYQFLGRTWDDLAKQLGLP 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830876  85 DFSPKSQDAVALQQIKERGALPMIDRGDIRQAIDRCSNIWASLPGAGYGQFEHKADSLIAKFKEAGG 151
Cdd:cd00736  75 DFSPESQDLAAIALIKERGALDDILAGRIEEAIAKLAKEWASLPGSGYGQPEHSMEELLAKYEKALG 141
Phage_lysozyme pfam00959
Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.
 33-140 2.17e-28

Phage lysozyme; This family includes lambda phage lysozyme and E. coli endolysin.


Pssm-ID: 395766 [Multi-domain]  Cd Length: 107  Bit Score: 100.89  E-value: 2.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830876    33 YDVIVGGELFTDYSDHPRKLvtlhpklKSTAAGRYQLLSRWWDAYRKQLGL-KDFSPKSQDAVALQQIKE----RGALPM 107
Cdd:pfam00959   1 YWTIGIGHNGKDVSPHPRAT-------KSEAAGRLQIDLDTAERCINQYHKvKDFNPNQQDALVSLAFNVgcgkRGFSTL 73

                          90       100       110
                  ....*....|....*....|....*....|....
gi 15830876   108 IDRGDIRQAIDRCSNIWASLP-GAGYGQFEHKAD 140
Cdd:pfam00959  74 LRAGNIGQWIKACSAIWKSLKaGKVYNGLVNRRE 107
Lyz-like cd00442
lysozyme-like domains; This family contains several members, including soluble lytic ...
 57-98 3.85e-05

lysozyme-like domains; This family contains several members, including soluble lytic transglycosylases (SLT), goose egg-white lysozymes (GEWL), hen egg-white lysozymes (HEWL), chitinases, bacteriophage lambda lysozymes, endolysins, autolysins, chitosanases, and pesticin. Typical members are involved in the hydrolysis of beta-1,4- linked polysaccharides.


Pssm-ID: 381596 [Multi-domain]  Cd Length: 59  Bit Score: 39.32  E-value: 3.85e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 15830876  57 PKLKSTAAGRYQLLSRWWDAYRKQLGLKDFSPKSQDAVALQQ 98
Cdd:cd00442  18 AGSGSGAAGLFQFMPGTWKAYGKNSSSDLNDPEASIEAAAKY 59
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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