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Links from Protein

Items: 18

1.

AAA family ATPase

This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop. (from Pfam)

Date:
2024-08-14
Family Accession:
NF025001.5
Method:
HMM
2.

P-loop NTPase

This family contains ATPases involved in plasmid partitioning [1]. It also contains the cytosolic Fe-S cluster assembling factor NBP35 which is required for biogenesis and export of both ribosomal subunits [2]. [1]. 2149583. A family of ATPases involved in active partitioning of diverse. bacterial plasmids.. Motallebi-Veshareh M, Rouch DA, Thomas CM;. Mol Microbiol 1990;4:1455-1463.. [2]. 15728363. The eukaryotic P loop NTPase Nbp35: an essential component of. the cytosolic and nuclear iron-sulfur protein assembly. machinery.. Hausmann A, Aguilar Netz DJ, Balk J, Pierik AJ, Muhlenhoff U,. Lill R;. Proc Natl Acad Sci U S A. 2005;102:3266-3271. (from Pfam)

Date:
2024-08-14
Family Accession:
NF022077.5
Method:
HMM
3.

division plane positioning ATPase MipZ

MipZ is an ATPase that forms a complex with the chromosome partitioning protein ParB near the chromosomal origin of replication [1]. It is responsible for the temporal and spatial regulation of FtsZ ring formation [1]. [1]. 16839883. MipZ, a spatial regulator coordinating chromosome segregation. with cell division in Caulobacter.. Thanbichler M, Shapiro L;. Cell. 2006;126:147-162. (from Pfam)

Date:
2024-08-14
Family Accession:
NF020704.5
Method:
HMM
4.

VirC1 protein

This family consists of several bacterial VirC1 proteins. In Agrobacterium tumefaciens, a cis-active 24-base-pair sequence adjacent to the right border of the T-DNA, called overdrive, stimulates tumour formation by increasing the level of T-DNA processing. It is thought that the virC operon which enhances T-DNA processing probably does so because the VirC1 protein interacts with overdrive. It has now been shown that the virC1 gene product binds to overdrive but not to the right border of T-DNA [1]. [1]. 2592351. The Agrobacterium tumefaciens virC1 gene product binds to. overdrive, a T-DNA transfer enhancer.. Toro N, Datta A, Carmi OA, Young C, Prusti RK, Nester EW;. J Bacteriol 1989;171:6845-6849. (from Pfam)

Date:
2024-08-14
Family Accession:
NF018691.5
Method:
HMM
5.

CobQ/CobB/MinD/ParA nucleotide binding domain

This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA Swiss:P29946 and CbiP Swiss:Q05597 from S.typhimurium [4], and CobQ Swiss:Q52686 from R. capsulatus [3]. These amidases catalyse amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria [4]. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family [6]. [1]. 9742225. Cobalamin (vitamin B12) biosynthesis: identification and. characterization of a Bacillus megaterium cobI operon.. Raux E, Lanois A, Warren MJ, Rambach A, Thermes C;. Biochem J 1998;335:159-166.. [2]. 9742226. Cobalamin (vitamin B12) biosynthesis: functional. characterization of the Bacillus megaterium cbi genes required. to convert uroporphyrinogen III into cobyrinic acid a,c-diamide.. Raux E, Lanois A, Rambach A, Warren MJ, Thermes C;. Biochem J 1998;335:167-173.. [3]. 7635831. Identification and sequence analysis of genes involved in late. steps in cobalamin (vitamin B12) synthesis in Rhodobacter. capsulatus.. Pollich M, Klug G;. J Bacteriol 1995;177:4481-4487.. [4]. 8501034. Characterization of the cobalamin (vitamin B12) biosynthetic. genes of Salmonella typhimurium.. Roth JR, Lawrence JG, Rubenfield M, Kieffer-Higgins S, Church. GM;. J Bacteriol 1993;175:3303-3316.. [5]. 10966576. The synthetase domains of cobalamin biosynthesis. amidotransferases cobB and cobQ belong to a . TRUNCATED at 1650 bytes (from Pfam)

Date:
2024-08-14
Family Accession:
NF013793.5
Method:
HMM
6.

SRP54-type protein, GTPase domain

This family includes relatives of the G-domain of the SRP54 family of proteins. [1]. 9002525. Crystal structure of the NG domain from the signal-recognition. particle receptor FtsY.. Montoya G, Svensson C, Luirink J, Sinning I;. Nature 1997;385:365-368. (from Pfam)

GO Terms:
Molecular Function:
GTP binding (GO:0005525)
Biological Process:
SRP-dependent cotranslational protein targeting to membrane (GO:0006614)
Date:
2024-08-14
Family Accession:
NF012662.5
Method:
HMM
7.
new record, indexing in progress
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new record, indexing in progress
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