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Links from Protein

Items: 7

1.
new record, indexing in progress
Family Accession:
2.
new record, indexing in progress
Family Accession:
3.

SPOCS_spoVID-N

Date:
2024-07-16
Family Accession:
NF044653.1
Method:
HMM
4.

LysM peptidoglycan-binding domain-containing protein

The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation [1]. This domain may have a general peptidoglycan binding function. The structure of this domain is known [2]. [1]. 1352512. Modular design of the Enterococcus hirae muramidase-2 and. Streptococcus faecalis autolysin.. Joris B, Englebert S, Chu CP, Kariyama R, Daneo-Moore L,. Shockman GD, Ghuysen JM;. FEMS Microbiol Lett 1992;70:257-264.. [2]. 10843862. The structure of a LysM domain from E. coli membrane-bound lytic. murein transglycosylase D (MltD).. Bateman A, Bycroft M;. J Mol Biol 2000;299:1113-1119. (from Pfam)

Date:
2024-07-09
Family Accession:
NF013630.4
Method:
HMM
5.
new record, indexing in progress
Family Accession:
6.

spore_VI_D family protein

spore_VI_D family protein

Date:
2017-03-02
Family Accession:
11495627
Method:
Sparcle
7.

stage VI sporulation protein D

SpoVID, the stage VI sporulation protein D, is restricted to endospore-forming members of the bacteria, all of which are found among the Firmicutes. It is widely distributed but not quite universal in this group. Between well-conserved N-terminal and C-terminal domains is a poorly conserved, low-complexity region of variable length, rich enough in glutamic acid to cause spurious BLAST search results unless a filter is used. The seed alignment for this model was trimmed, in effect, by choosing member sequences in which these regions are relatively short. SpoVID is involved in spore coat assembly by the mother cell compartment late in the process of sporulation.

Gene:
spoVID
GO Terms:
Molecular Function:
molecular_function (GO:0003674)
Biological Process:
asexual sporulation (GO:0030436)
Date:
2021-04-27
Family Accession:
TIGR02907.1
Method:
HMM
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