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Links from Protein

Items: 16

1.

cell division FtsA domain-containing protein

FtsA is essential for bacterial cell division, and co-localises to the septal ring with FtsZ. It has been suggested that the interaction of FtsA-FtsZ has arisen through coevolution in different bacterial strains [1]. The FtsA protein contains two structurally related actin-like ATPase domains which are also structurally related to the ATPase domains of HSP70 (see PF00012). FtsA has a SHS2 domain PF02491 inserted in to the RnaseH fold PF02491 [2]. [1]. 9352931. Interactions between heterologous FtsA and FtsZ proteins at the. FtsZ ring.. Ma X, Sun Q, Wang R, Singh G, Jonietz EL, Margolin W;. J Bacteriol 1997;179:6788-6797.. [2]. 15281131. The SHS2 module is a common structural theme in functionally. diverse protein groups, like Rpb7p, FtsA, GyrI, and. MTH1598/TM1083 superfamilies.. Anantharaman V, Aravind L;. Proteins. 2004;56:795-807. (from Pfam)

Date:
2024-08-14
Family Accession:
NF025806.5
Method:
HMM
2.

rod shape-determining protein

This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl [1]. [1]. 12758091. Cytoskeletons in prokaryotes.. Mayer F;. Cell Biol Int 2003;27:429-438. (from Pfam)

Date:
2024-08-14
Family Accession:
NF018435.5
Method:
HMM
3.

Hsp70 family protein

Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region. [1]. 9476895. The Hsp70 and Hsp60 chaperone machines.. Bukau B, Horwich AL;. Cell 1998;92:351-366. (from Pfam)

GO Terms:
Molecular Function:
ATP binding (GO:0005524)
Molecular Function:
ATP-dependent protein folding chaperone (GO:0140662)
Date:
2024-08-14
Family Accession:
NF012242.5
Method:
HMM
4.

Actin

Date:
2024-08-14
Family Accession:
NF012252.5
Method:
HMM
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.
new record, indexing in progress
Family Accession:
11.
new record, indexing in progress
Family Accession:
12.

rod shape-determining protein

rod shape-determining protein assembles into large fibrous spirals beneath the cell membrane and determines the shape of rod-like bacterial cells

Date:
2023-03-03
Family Accession:
11487002
Method:
Sparcle
13.

rod shape-determining protein MreB

Gene:
mreB
Date:
2021-05-18
Family Accession:
NBR007264
Method:
BlastRule
14.
new record, indexing in progress
Family Accession:
15.

rod shape-determining protein MreB

Gene:
mreB
Date:
2020-10-26
Family Accession:
NF010539.0
Method:
HMM
16.

MreB/Mrl family cell shape determining protein

MreB (mecillinam resistance) in E. coli (also called envB) and the paralogous pair MreB and Mrl of Bacillus subtilis have all been shown to help determine cell shape. This protein is present in a wide variety of bacteria, including spirochetes, but is missing from the Mycoplasmas and from Gram-positive cocci. Most completed bacterial genomes have a single member of this family. In some species it is an essential gene. A close homolog is found in the Archaeon Methanobacterium thermoautotrophicum, and a more distant homolog in Archaeoglobus fulgidus. The family is related to cell division protein FtsA and heat shock protein DnaK.

GO Terms:
Biological Process:
cell morphogenesis (GO:0000902)
Date:
2024-05-16
Family Accession:
TIGR00904.1
Method:
HMM
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