stage II sporulation protein M (SpoIIM) is one of four stage II sporulation proteins that is necessary for the forespore inside the mother-cell to be properly internalized through the breakdown of peptidoglycans trapped between the membranes of the septum separating the forespore and the mother-cell
Stage II sporulation protein M; SpoIIM is on e of four stage II sporulation proteins that is ...
6-203
1.37e-51
Stage II sporulation protein M; SpoIIM is on e of four stage II sporulation proteins that is necessary for the forespore inside the mother-cell to be properly internalized through the breakdown of peptidoglycans trapped between the membranes of the septum separating the forespore and the mother-cell. The four proteins working in sequence are SpoIIB, pfam05036, SpoIIM, SpoIIP, pfam07454, and finally SpoIID, pfam08486. D, M and P are in a complex with each other and the complex assembles in a hierarchical manner such that M, which serves as a membrane anchor, recruits P to the septum and P, in turn, recruits D to the septum.
The actual alignment was detected with superfamily member TIGR02831:
Pssm-ID: 469827 Cd Length: 200 Bit Score: 165.13 E-value: 1.37e-51
stage II sporulation protein M; A comparative genome analysis of all sequenced genomes of ...
6-203
1.37e-51
stage II sporulation protein M; A comparative genome analysis of all sequenced genomes of shows a number of proteins conserved strictly among the endospore-forming subset of the Firmicutes. This predicted integral membrane protein is designated stage II sporulation protein M. [Cellular processes, Sporulation and germination]
Pssm-ID: 131878 Cd Length: 200 Bit Score: 165.13 E-value: 1.37e-51
Stage II sporulation protein M; SpoIIM is on e of four stage II sporulation proteins that is ...
23-199
5.85e-24
Stage II sporulation protein M; SpoIIM is on e of four stage II sporulation proteins that is necessary for the forespore inside the mother-cell to be properly internalized through the breakdown of peptidoglycans trapped between the membranes of the septum separating the forespore and the mother-cell. The four proteins working in sequence are SpoIIB, pfam05036, SpoIIM, SpoIIP, pfam07454, and finally SpoIID, pfam08486. D, M and P are in a complex with each other and the complex assembles in a hierarchical manner such that M, which serves as a membrane anchor, recruits P to the septum and P, in turn, recruits D to the septum.
Pssm-ID: 426524 Cd Length: 173 Bit Score: 93.50 E-value: 5.85e-24
stage II sporulation protein M; A comparative genome analysis of all sequenced genomes of ...
6-203
1.37e-51
stage II sporulation protein M; A comparative genome analysis of all sequenced genomes of shows a number of proteins conserved strictly among the endospore-forming subset of the Firmicutes. This predicted integral membrane protein is designated stage II sporulation protein M. [Cellular processes, Sporulation and germination]
Pssm-ID: 131878 Cd Length: 200 Bit Score: 165.13 E-value: 1.37e-51
Stage II sporulation protein M; SpoIIM is on e of four stage II sporulation proteins that is ...
23-199
5.85e-24
Stage II sporulation protein M; SpoIIM is on e of four stage II sporulation proteins that is necessary for the forespore inside the mother-cell to be properly internalized through the breakdown of peptidoglycans trapped between the membranes of the septum separating the forespore and the mother-cell. The four proteins working in sequence are SpoIIB, pfam05036, SpoIIM, SpoIIP, pfam07454, and finally SpoIID, pfam08486. D, M and P are in a complex with each other and the complex assembles in a hierarchical manner such that M, which serves as a membrane anchor, recruits P to the septum and P, in turn, recruits D to the septum.
Pssm-ID: 426524 Cd Length: 173 Bit Score: 93.50 E-value: 5.85e-24
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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Functional characterization of the conserved domain architecture found on the query.
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