stage II sporulation protein SpoIIP
Protein Classification
stage II sporulation protein P( domain architecture ID 10021552)
stage II sporulation protein P is an autolysin that is involved in the engulfment of the developing spore (the forespore) by the adjacent mother cell during the conversion of a growing cell into an endospore
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| SpoIIP | COG5819 | Stage II sporulation protein SpoIIP, required for dissolution of the septal cell wall [Cell ... |
100-378 | 2.90e-100 | |||||
Stage II sporulation protein SpoIIP, required for dissolution of the septal cell wall [Cell cycle control, cell division, chromosome partitioning]; : Pssm-ID: 444521 [Multi-domain] Cd Length: 256 Bit Score: 297.61 E-value: 2.90e-100
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| Name | Accession | Description | Interval | E-value | |||||
| SpoIIP | COG5819 | Stage II sporulation protein SpoIIP, required for dissolution of the septal cell wall [Cell ... |
100-378 | 2.90e-100 | |||||
Stage II sporulation protein SpoIIP, required for dissolution of the septal cell wall [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 444521 [Multi-domain] Cd Length: 256 Bit Score: 297.61 E-value: 2.90e-100
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| spore_II_P | TIGR02867 | stage II sporulation protein P; Stage II sporulation protein P is a protein of the endospore ... |
173-377 | 4.63e-100 | |||||
stage II sporulation protein P; Stage II sporulation protein P 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. SpoIIP, along with SpoIIM and SpoIID, is one of three major proteins involved in engulfment of the forespore by the mother cell. This protein family is named for the single member in Bacillus subtilis, although most sporulating bacteria have two members. [Cellular processes, Sporulation and germination] Pssm-ID: 274330 Cd Length: 196 Bit Score: 294.98 E-value: 4.63e-100
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| SpoIIP | pfam07454 | Stage II sporulation protein P (SpoIIP); This family contains the bacterial stage II ... |
96-373 | 2.63e-92 | |||||
Stage II sporulation protein P (SpoIIP); This family contains the bacterial stage II sporulation protein P (SpoIIP) (approximately 350 residues long). It has been shown that a block in polar cytokinesis in Bacillus subtilis is mediated partly by transcription of spoIID, spoIIM and spoIIP. This inhibition of polar division is involved in the locking in of asymmetry after the formation of a polar septum during sporulation. Engulfment in Bacillus subtilis is mediated by two complementary systems: the first includes the proteins SpoIID, SpoIIM and SpoIIP (DMP) which carry out the engulfment, and the second includes the SpoIIQ-SpoIIIAGH (Q-AH) zipper, that recruits other proteins to the septum in a second-phase of the engulfment. The course of events follows as the incorporation firstly of SpoIIB into the septum during division to serve directly or indirectly as a landmark for localising SpoIIM and then SpoIIP and SpoIID to the septum. SpoIIP and SpoIID interact together to form part of the DMP complex. SpoIIP itself has been identified as an autolysin with peptidoglycan hydrolase activity. Pssm-ID: 462168 Cd Length: 263 Bit Score: 277.68 E-value: 2.63e-92
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| MurNAc-LAA | cd02696 | N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, ... |
298-371 | 1.19e-04 | |||||
N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall. Pssm-ID: 119407 [Multi-domain] Cd Length: 172 Bit Score: 42.14 E-value: 1.19e-04
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| Name | Accession | Description | Interval | E-value | |||||
| SpoIIP | COG5819 | Stage II sporulation protein SpoIIP, required for dissolution of the septal cell wall [Cell ... |
100-378 | 2.90e-100 | |||||
Stage II sporulation protein SpoIIP, required for dissolution of the septal cell wall [Cell cycle control, cell division, chromosome partitioning]; Pssm-ID: 444521 [Multi-domain] Cd Length: 256 Bit Score: 297.61 E-value: 2.90e-100
|
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| spore_II_P | TIGR02867 | stage II sporulation protein P; Stage II sporulation protein P is a protein of the endospore ... |
173-377 | 4.63e-100 | |||||
stage II sporulation protein P; Stage II sporulation protein P 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. SpoIIP, along with SpoIIM and SpoIID, is one of three major proteins involved in engulfment of the forespore by the mother cell. This protein family is named for the single member in Bacillus subtilis, although most sporulating bacteria have two members. [Cellular processes, Sporulation and germination] Pssm-ID: 274330 Cd Length: 196 Bit Score: 294.98 E-value: 4.63e-100
|
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| SpoIIP | pfam07454 | Stage II sporulation protein P (SpoIIP); This family contains the bacterial stage II ... |
96-373 | 2.63e-92 | |||||
Stage II sporulation protein P (SpoIIP); This family contains the bacterial stage II sporulation protein P (SpoIIP) (approximately 350 residues long). It has been shown that a block in polar cytokinesis in Bacillus subtilis is mediated partly by transcription of spoIID, spoIIM and spoIIP. This inhibition of polar division is involved in the locking in of asymmetry after the formation of a polar septum during sporulation. Engulfment in Bacillus subtilis is mediated by two complementary systems: the first includes the proteins SpoIID, SpoIIM and SpoIIP (DMP) which carry out the engulfment, and the second includes the SpoIIQ-SpoIIIAGH (Q-AH) zipper, that recruits other proteins to the septum in a second-phase of the engulfment. The course of events follows as the incorporation firstly of SpoIIB into the septum during division to serve directly or indirectly as a landmark for localising SpoIIM and then SpoIIP and SpoIID to the septum. SpoIIP and SpoIID interact together to form part of the DMP complex. SpoIIP itself has been identified as an autolysin with peptidoglycan hydrolase activity. Pssm-ID: 462168 Cd Length: 263 Bit Score: 277.68 E-value: 2.63e-92
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| MurNAc-LAA | cd02696 | N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, ... |
298-371 | 1.19e-04 | |||||
N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall. Pssm-ID: 119407 [Multi-domain] Cd Length: 172 Bit Score: 42.14 E-value: 1.19e-04
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