SpoIID/LytB domain-containing protein similar to Bacillus subtilis stage II sporulation protein D (spoIID) that may act at the level of sigma-G activity or its stability| cell wall-binding repeat-containing protein similar to Clostridium difficile S-layer protein SlpA, cell wall protein V (CwpV), and Cwp66; the cell wall binding repeat 2 is found in mutiple copies in proteins
SpoIID/LytB domain; This model describes a domain found typically in two or three proteins per ...
412-701
4.84e-78
SpoIID/LytB domain; This model describes a domain found typically in two or three proteins per genome in Cyanobacteria and Firmicutes, and sporadically in other genomes. One member is SpoIID of Bacillus subtilis. Another in B. subtilis is the C-terminal half of LytB, encoded immediately upstream of an amidase, the autolysin LytC, to which its N-terminus is homologous. Gene neighborhoods are not well conserved for members of this family, as many, such as SpoIID, are monocistronic. One early modelling-based study suggests a DNA-binding role for SpoIID, but the function of this domain is unknown. [Unknown function, General]
Pssm-ID: 274252 [Multi-domain] Cd Length: 267 Bit Score: 250.45 E-value: 4.84e-78
Stage II sporulation protein; This domain is found in the stage II sporulation protein SpoIID. ...
403-486
7.19e-29
Stage II sporulation protein; This domain is found in the stage II sporulation protein SpoIID. SpoIID is necessary for membrane migration as well as for some of the earlier steps in engulfment during bacterial endospore formation. The domain is also found in amidase enhancer proteins. Amidases, like SpoIID, are cell wall hydrolases.
Pssm-ID: 462491 [Multi-domain] Cd Length: 100 Bit Score: 110.77 E-value: 7.19e-29
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide ...
162-235
1.65e-13
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide variety of bacterial cell surface proteins. It has been show the three tandem repeats of the CWB2 domain are essential for correct anchoring to the cell wall. It was shown that in SlpA and Cwp2 that these domains were essential for the binding of PSII an anionic teichoic acid-like component of the cell wall. The structure of the Cwp8 and Cwp6 proteins shows that this domain forms a trimeric arrangement with each domain adopting a structure with some similarity to the Toprim fold. A groove containing many conserved residues was predicted to be the site of the PSII molecule.
Pssm-ID: 461185 [Multi-domain] Cd Length: 80 Bit Score: 66.01 E-value: 1.65e-13
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide ...
252-337
5.20e-09
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide variety of bacterial cell surface proteins. It has been show the three tandem repeats of the CWB2 domain are essential for correct anchoring to the cell wall. It was shown that in SlpA and Cwp2 that these domains were essential for the binding of PSII an anionic teichoic acid-like component of the cell wall. The structure of the Cwp8 and Cwp6 proteins shows that this domain forms a trimeric arrangement with each domain adopting a structure with some similarity to the Toprim fold. A groove containing many conserved residues was predicted to be the site of the PSII molecule.
Pssm-ID: 461185 [Multi-domain] Cd Length: 80 Bit Score: 53.30 E-value: 5.20e-09
SpoIID/LytB domain; This model describes a domain found typically in two or three proteins per ...
412-701
4.84e-78
SpoIID/LytB domain; This model describes a domain found typically in two or three proteins per genome in Cyanobacteria and Firmicutes, and sporadically in other genomes. One member is SpoIID of Bacillus subtilis. Another in B. subtilis is the C-terminal half of LytB, encoded immediately upstream of an amidase, the autolysin LytC, to which its N-terminus is homologous. Gene neighborhoods are not well conserved for members of this family, as many, such as SpoIID, are monocistronic. One early modelling-based study suggests a DNA-binding role for SpoIID, but the function of this domain is unknown. [Unknown function, General]
Pssm-ID: 274252 [Multi-domain] Cd Length: 267 Bit Score: 250.45 E-value: 4.84e-78
stage II sporulation protein D; Stage II sporulation protein D (SpoIID) is a protein of the ...
412-702
2.86e-54
stage II sporulation protein D; Stage II sporulation protein D (SpoIID) is a protein of the endospore formation program in a number of lineages in the Firmicutes (low-GC Gram-positive bacteria). It is expressed in the mother cell compartment, under control of Sigma-E. SpoIID, along with SpoIIM and SpoIIP, is one of three major proteins involved in engulfment of the forespore by the mother cell. [Cellular processes, Sporulation and germination]
Pssm-ID: 274332 [Multi-domain] Cd Length: 338 Bit Score: 189.54 E-value: 2.86e-54
Stage II sporulation protein; This domain is found in the stage II sporulation protein SpoIID. ...
403-486
7.19e-29
Stage II sporulation protein; This domain is found in the stage II sporulation protein SpoIID. SpoIID is necessary for membrane migration as well as for some of the earlier steps in engulfment during bacterial endospore formation. The domain is also found in amidase enhancer proteins. Amidases, like SpoIID, are cell wall hydrolases.
Pssm-ID: 462491 [Multi-domain] Cd Length: 100 Bit Score: 110.77 E-value: 7.19e-29
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide ...
162-235
1.65e-13
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide variety of bacterial cell surface proteins. It has been show the three tandem repeats of the CWB2 domain are essential for correct anchoring to the cell wall. It was shown that in SlpA and Cwp2 that these domains were essential for the binding of PSII an anionic teichoic acid-like component of the cell wall. The structure of the Cwp8 and Cwp6 proteins shows that this domain forms a trimeric arrangement with each domain adopting a structure with some similarity to the Toprim fold. A groove containing many conserved residues was predicted to be the site of the PSII molecule.
Pssm-ID: 461185 [Multi-domain] Cd Length: 80 Bit Score: 66.01 E-value: 1.65e-13
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide ...
64-149
4.60e-12
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide variety of bacterial cell surface proteins. It has been show the three tandem repeats of the CWB2 domain are essential for correct anchoring to the cell wall. It was shown that in SlpA and Cwp2 that these domains were essential for the binding of PSII an anionic teichoic acid-like component of the cell wall. The structure of the Cwp8 and Cwp6 proteins shows that this domain forms a trimeric arrangement with each domain adopting a structure with some similarity to the Toprim fold. A groove containing many conserved residues was predicted to be the site of the PSII molecule.
Pssm-ID: 461185 [Multi-domain] Cd Length: 80 Bit Score: 62.16 E-value: 4.60e-12
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide ...
252-337
5.20e-09
ell wall binding domain 2 (CWB2); This domain is found in 1 to 3 tandem copies in a wide variety of bacterial cell surface proteins. It has been show the three tandem repeats of the CWB2 domain are essential for correct anchoring to the cell wall. It was shown that in SlpA and Cwp2 that these domains were essential for the binding of PSII an anionic teichoic acid-like component of the cell wall. The structure of the Cwp8 and Cwp6 proteins shows that this domain forms a trimeric arrangement with each domain adopting a structure with some similarity to the Toprim fold. A groove containing many conserved residues was predicted to be the site of the PSII molecule.
Pssm-ID: 461185 [Multi-domain] Cd Length: 80 Bit Score: 53.30 E-value: 5.20e-09
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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