Protein Family Models for Protein (Select 1248552692) - Protein Family Models

Select item 4161351.

Septum formation inhibitor MinC, N-terminal domain

In Escherichia coli Swiss:P06138 assembles into a Z ring at midcell while assembly at polar sites is prevented by the min system. MinC Swiss:P18196 a component of this system, is an inhibitor of FtsZ assembly that is positioned within the cell by interaction with MinDE. MinC is an oligomer, probably a dimer [1]. The C terminal half of MinC is the most conserved and interacts with MinD. The N terminal half is thought to interact with FtsZ. [1]. 10869074. Analysis of MinC reveals two independent domains involved in interaction with MinD and FtsZ. Hu Z, Lutkenhaus J;. J Bacteriol 2000;182:3965-3971. [2]. 10611296. The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization. Hu Z, Mukherjee A, Pichoff S, Lutkenhaus J;. Proc Natl Acad Sci U S A 1999;96:14819-14824. [3]. 11350934. Crystal structure of the bacterial cell division inhibitor MinC. Cordell SC, Anderson RE, Lowe J;. EMBO J 2001;20:2454-2461. (from Pfam)

GO Terms:

Biological Process:: regulation of cell division (GO:0051302)

Date:: 2024-10-16

Family Accession:: NF017059.5
Method:: HMM

Select item 4131322.

septum site-determining protein MinC

In Escherichia coli Swiss:P06138 assembles into a Z ring at midcell while assembly at polar sites is prevented by the min system. MinC Swiss:P18196 a component of this system, is an inhibitor of FtsZ assembly that is positioned within the cell by interaction with MinDE. MinC is an oligomer, probably a dimer [1]. The C terminal half of MinC is the most conserved and interacts with MinD. The N terminal half is thought interact with FtsZ. [1]. 10869074. Analysis of MinC reveals two independent domains involved in interaction with MinD and FtsZ. Hu Z, Lutkenhaus J;. J Bacteriol 2000;182:3965-3971. [2]. 10611296. The MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization. Hu Z, Mukherjee A, Pichoff S, Lutkenhaus J;. Proc Natl Acad Sci U S A 1999;96:14819-14824. (from Pfam)

GO Terms:

Biological Process:: cell morphogenesis (GO:0000902)

Date:: 2024-10-16

Family Accession:: NF015716.5
Method:: HMM

Select item 3926083.

new record, indexing in progress

Family Accession:

Select item 3916864.

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Family Accession:

Select item 3518855.

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Family Accession:

Select item 3495376.

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Family Accession:

Select item 1415107.

septum site-determining protein MinC

MinC assists in correct placement of the septum for cell division by inhibiting septum formation at other sites. Note that this model hits broadly but not universally; MinC equivalents from Deinocoocus, Synechocystis PCC 6803, and Helicobacter pylori, for example, do not hit the full length of the model, may score between the trusted and noise cutoffs, and must be handled in annotation pipelines by protein family models other than this one.

Gene:: minC

GO Terms:

Biological Process:: division septum site selection (GO:0000918)

Molecular Function:: enzyme inhibitor activity (GO:0004857)

Biological Process:: regulation of cell septum assembly (GO:1901891)

Date:: 2024-06-27

Family Accession:: TIGR01222.1
Method:: HMM

Select item 515898.

septum site-determining protein MinC

septum site-determining protein MinC is a cell division inhibitor that blocks the formation of polar Z ring septa

Date:: 2023-03-06

Family Accession:: 11436700
Method:: Sparcle

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