Protein Family Models

This domain is found at the C-terminal end of Protein adenylyltransferase SoFic from Shewanella oneidensis and similar bacterial sequences. SoFic mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins. This is a winged-helix DNA-binding domain often found associated with Pfam:PF02661 [1-3]. Paper describing PDB structure 3eqx. [1]. 19127588. Crystal structure of the Fic (Filamentation induced by cAMP) family protein SO4266 (gi|24375750) from Shewanella oneidensis MR-1 at 1.6 A resolution. Das D, Krishna SS, McMullan D, Miller MD, Xu Q, Abdubek P, Acosta C, Astakhova T, Axelrod HL, Burra P, Carlton D, Chiu HJ, Clayton T, Deller MC, Duan L, Elias Y, Elsliger MA, Ernst D, Feuerhelm J, Grzechnik A, Grzechnik SK, Hale J, Han GW, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Kozbial P, Kumar A, Marciano D, Morse AT, Murphy KD, Nigoghossian E, Okach L, Oommachen S, Paulsen J, Reyes R, Rife CL, Sefcovic N, Tien H, Trame CB, Trout CV, van den Bedem H, Weekes D, White A, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, Wilson IA;. Proteins. 2009;75:264-271. Paper describing PDB structure 3zcn. [2]. 23738009. Conserved inhibitory mechanism and competent ATP binding mode for adenylyltransferases with Fic fold. Goepfert A, Stanger FV, Dehio C, Schirmer T;. PLoS One. 2013;8:e64901. [3]. 22266942. Adenylylation control by intra- or intermolecular active-site obstruction in Fic proteins. Engel P, Goepfert A, Stanger FV, Harms A, Schmidt A, Schirmer T, Dehio C;. Nature. 2012;482:107-110. (from Pfam)

Date:

2024-10-16

This domain is found at the N-terminus of the Fic/DOC family, Pfam:PF02661. (from Pfam)

Date:

2024-08-14

This family consists of the Fic (filamentation induced by cAMP) protein and doc (death on curing). The Fic protein is involved in cell division and is suggested to be involved in the synthesis of PAB or folate, indicating that the Fic protein and cAMP are involved in a regulatory mechanism of cell division via folate metabolism [1]. This family contains a central conserved motif HPFXXGNG in most members. The exact molecular function of these proteins is uncertain. P1 lysogens of Escherichia coli carry the prophage as a stable low copy number plasmid. The frequency with which viable cells cured of prophage are produced is about 10(-5) per cell per generation [1]. A significant part of this remarkable stability can be attributed to a plasmid-encoded mechanism that causes death of cells that have lost P1 [2]. In other words, the lysogenic cells appear to be addicted to the presence of the prophage. The plasmid withdrawal response depends on a gene named doc (death on curing) that is represented by this family [2]. Doc induces a reversible growth arrest of E. coli cells by targetting the protein synthesis machinery. Doc hosts the C-terminal domain of its antitoxin partner Phd (prevents host death) through fold complementation, a domain that is intrinsically disordered in solution but that folds into an alpha-helix on binding to Doc [3].This domain forms complexes with Phd antitoxins containing Pfam:PF02604. [1]. 1656497. Functional analysis of the fic gene involved in regulation of cell division. Komano T, Utsumi R, Kawamukai M;. Res Microbiol 1991;142:269-277. [2]. 8411153. Plasmid addiction genes of bacteriophage P1: do. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

Fic (Filamentation induced by cAMP) family protein similar to Shewanella oneidensis adenosine monophosphate-protein transferase SoFic, which mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins

Date:

2024-06-29