NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|157850190|gb|ABV89928|]
View 

spoVID-dependent spore coat assembly factor, partial [Bacillus subtilis subsp. subtilis]

Protein Classification

LysM family protein( domain architecture ID 11443400)

LysM family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
1-30 9.33e-12

LysM repeat [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 54.71  E-value: 9.33e-12
                         10        20        30
                 ....*....|....*....|....*....|
gi 157850190   1 MKIHIVQKGDSLWKIAEKYGVDVEEVKKLN 30
Cdd:COG1388  109 PVTYTVKKGDTLWSIARRYGVSVEELKRWN 138
 
Name Accession Description Interval E-value
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
1-30 9.33e-12

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 54.71  E-value: 9.33e-12
                         10        20        30
                 ....*....|....*....|....*....|
gi 157850190   1 MKIHIVQKGDSLWKIAEKYGVDVEEVKKLN 30
Cdd:COG1388  109 PVTYTVKKGDTLWSIARRYGVSVEELKRWN 138
spore_safA TIGR02899
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ...
 6-34 2.27e-11

spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found at the interface of the spore cortex and spore coat, and is dependent on SpoVID for its localization. This model is based on the N-terminal LysM (lysin motif) domain (see pfamAM model pfam01476) of SafA and, from several other spore-forming species, the protein with the most similar N-terminal region. However, this set of proteins differs greatly in C-terminal of the LysM domaim; blocks of 12-residue and 13-residue repeats are found in the Bacillus cereus group, tandem LysM domains in Thermoanaerobacter tengcongensis MB4, etc. in which one of which is found in most examples of endospore-forming bacteria. [Cellular processes, Sporulation and germination]


Pssm-ID: 131945 [Multi-domain]  Cd Length: 44  Bit Score: 50.95  E-value: 2.27e-11
                         10        20
                 ....*....|....*....|....*....
gi 157850190   6 VQKGDSLWKIAEKYGVDVEEVKKLNTQLS 34
Cdd:TIGR02899  1 VQKGDTLWKIAKKYGVDFDELIQANPQLS 29
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 2-30 9.31e-11

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 49.41  E-value: 9.31e-11
                        10        20
                ....*....|....*....|....*....
gi 157850190  2 KIHIVQKGDSLWKIAEKYGVDVEEVKKLN 30
Cdd:cd00118   1 KTYTVKPGDTLWSIAKKYGVTVEELAAAN 29
LysM smart00257
Lysin motif;
3-34 4.15e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 45.13  E-value: 4.15e-09
                          10        20        30
                  ....*....|....*....|....*....|..
gi 157850190    3 IHIVQKGDSLWKIAEKYGVDVEEVKKLNTQLS 34
Cdd:smart00257  1 TYTVKKGDTLSSIARRYGISVSDLLELNNILD 32
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 4-30 7.88e-09

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 44.31  E-value: 7.88e-09
                         10        20
                 ....*....|....*....|....*..
gi 157850190   4 HIVQKGDSLWKIAEKYGVDVEEVKKLN 30
Cdd:pfam01476  1 YTVKKGDTLSSIAKRYGITVEQLAELN 27
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
2-30 6.15e-06

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 39.68  E-value: 6.15e-06
                         10        20
                 ....*....|....*....|....*....
gi 157850190   2 KIHIVQKGDSLWKIAEKYGVDVEEVKKLN 30
Cdd:PRK06347 331 KIYTVVKGDSLWRIANNHKVTVANLKAWN 359
 
Name Accession Description Interval E-value
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
1-30 9.33e-12

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 54.71  E-value: 9.33e-12
                         10        20        30
                 ....*....|....*....|....*....|
gi 157850190   1 MKIHIVQKGDSLWKIAEKYGVDVEEVKKLN 30
Cdd:COG1388  109 PVTYTVKKGDTLWSIARRYGVSVEELKRWN 138
spore_safA TIGR02899
spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found ...
 6-34 2.27e-11

spore coat assembly protein SafA; SafA (YrbB) (SafA) of Bacillus subtilis is a protein found at the interface of the spore cortex and spore coat, and is dependent on SpoVID for its localization. This model is based on the N-terminal LysM (lysin motif) domain (see pfamAM model pfam01476) of SafA and, from several other spore-forming species, the protein with the most similar N-terminal region. However, this set of proteins differs greatly in C-terminal of the LysM domaim; blocks of 12-residue and 13-residue repeats are found in the Bacillus cereus group, tandem LysM domains in Thermoanaerobacter tengcongensis MB4, etc. in which one of which is found in most examples of endospore-forming bacteria. [Cellular processes, Sporulation and germination]


Pssm-ID: 131945 [Multi-domain]  Cd Length: 44  Bit Score: 50.95  E-value: 2.27e-11
                         10        20
                 ....*....|....*....|....*....
gi 157850190   6 VQKGDSLWKIAEKYGVDVEEVKKLNTQLS 34
Cdd:TIGR02899  1 VQKGDTLWKIAKKYGVDFDELIQANPQLS 29
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 2-30 9.31e-11

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 49.41  E-value: 9.31e-11
                        10        20
                ....*....|....*....|....*....
gi 157850190  2 KIHIVQKGDSLWKIAEKYGVDVEEVKKLN 30
Cdd:cd00118   1 KTYTVKPGDTLWSIAKKYGVTVEELAAAN 29
LysM smart00257
Lysin motif;
3-34 4.15e-09

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 45.13  E-value: 4.15e-09
                          10        20        30
                  ....*....|....*....|....*....|..
gi 157850190    3 IHIVQKGDSLWKIAEKYGVDVEEVKKLNTQLS 34
Cdd:smart00257  1 TYTVKKGDTLSSIARRYGISVSDLLELNNILD 32
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 4-30 7.88e-09

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 44.31  E-value: 7.88e-09
                         10        20
                 ....*....|....*....|....*..
gi 157850190   4 HIVQKGDSLWKIAEKYGVDVEEVKKLN 30
Cdd:pfam01476  1 YTVKKGDTLSSIAKRYGITVEQLAELN 27
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 2-30 2.91e-06

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 40.37  E-value: 2.91e-06
                         10        20        30
                 ....*....|....*....|....*....|..
gi 157850190   2 KIHIVQKGDSLWKIAEKY---GVDVEEVKKLN 30
Cdd:COG1652  110 KTYTVKPGDTLWGIAKRFygdPARWPEIAEAN 141
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
2-30 6.15e-06

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 39.68  E-value: 6.15e-06
                         10        20
                 ....*....|....*....|....*....
gi 157850190   2 KIHIVQKGDSLWKIAEKYGVDVEEVKKLN 30
Cdd:PRK06347 331 KIYTVVKGDSLWRIANNHKVTVANLKAWN 359
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
2-30 1.64e-05

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 38.52  E-value: 1.64e-05
                         10        20
                 ....*....|....*....|....*....
gi 157850190   2 KIHIVQKGDSLWKIAEKYGVDVEEVKKLN 30
Cdd:PRK06347 480 KVYTVAKGDSLWRIANNNKVTIANLKSWN 508
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
2-30 2.79e-05

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 37.75  E-value: 2.79e-05
                         10        20
                 ....*....|....*....|....*....
gi 157850190   2 KIHIVQKGDSLWKIAEKYGVDVEEVKKLN 30
Cdd:PRK06347 406 KVYTVVKGDSLWRIANNNKVTIANLKSWN 434
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
2-30 5.04e-05

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 36.98  E-value: 5.04e-05
                         10        20
                 ....*....|....*....|....*....
gi 157850190   2 KIHIVQKGDSLWKIAEKYGVDVEEVKKLN 30
Cdd:PRK06347 548 KTYTVKKGDSLWAISRQYKTTVDNIKAWN 576
PRK13914 PRK13914
invasion associated endopeptidase;
4-30 3.86e-04

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 34.78  E-value: 3.86e-04
                         10        20
                 ....*....|....*....|....*..
gi 157850190   4 HIVQKGDSLWKIAEKYGVDVEEVKKLN 30
Cdd:PRK13914 202 HAVKSGDTIWALSVKYGVSVQDIMSWN 228
PRK13914 PRK13914
invasion associated endopeptidase;
5-30 4.34e-04

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 34.39  E-value: 4.34e-04
                         10        20
                 ....*....|....*....|....*.
gi 157850190   5 IVQKGDSLWKIAEKYGVDVEEVKKLN 30
Cdd:PRK13914  31 VVEAGDTLWGIAQSKGTTVDAIKKAN 56
PRK11198 PRK11198
LysM domain/BON superfamily protein; Provisional
 4-19 4.89e-04

LysM domain/BON superfamily protein; Provisional


Pssm-ID: 236880 [Multi-domain]  Cd Length: 147  Bit Score: 34.12  E-value: 4.89e-04
                         10
                 ....*....|....*.
gi 157850190   4 HIVQKGDSLWKIAEKY 19
Cdd:PRK11198  98 YTVKSGDTLSAIAKKV 113
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 6-34 1.74e-03

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 32.78  E-value: 1.74e-03
                         10        20
                 ....*....|....*....|....*....
gi 157850190   6 VQKGDSLWKIAEKYGVDVEEVKKLNTQLS 34
Cdd:PRK10783 407 VRKGDSLSSIAKRHGVNIKDVMRWNSDTA 435
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH