E. coli cells producing FtsA-GFP, which localizes to the cell division site.
Identifiers
Organism
Escherichia coli (strain K12)
Symbol
FtsA
Entrez
944778
RefSeq (Prot)
NP_414636.1
UniProt
P0ABH0
Other data
Chromosome
Genome: 0.1 - 0.11 Mb
Search for
Structures
Swiss-model
Domains
InterPro
FtsA
Identifiers
Symbol
FtsA
InterPro
IPR020823
SHS2 "1C" domain inserted in FtsA
Identifiers
Symbol
SHS2_FtsA
Pfam
PF02491
InterPro
IPR003494
SMART
SM00842
Available protein structures:
Pfam
structures / ECOD
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
FtsA is a bacterial protein that is related to actin by overall structural similarity and in its ATP binding pocket.[1][2][3]
Along with other bacterial actin homologs such as MreB, ParM, and MamK, these proteins suggest that eukaryotic actin has a common ancestry. Like the other bacterial actins, FtsA binds ATP and can form actin-like filaments.[4] The FtsA-FtsA interface has been defined by structural as well as genetic analysis.[5] Although present in many diverse Gram-positive and Gram-negative species, FtsA is absent in actinobacteria and cyanobacteria. FtsA also is structurally similar to PilM, a type IV pilus ATPase.[6]
^van den Ent F, Löwe J (Oct 2000). "Crystal structure of the cell division protein FtsA from Thermotoga maritima". The EMBO Journal. 19 (20): 5300–7. doi:10.1093/emboj/19.20.5300. PMC 313995. PMID 11032797.
^Gunning PW, Ghoshdastider U, Whitaker S, Popp D, Robinson RC (Jun 2015). "The evolution of compositionally and functionally distinct actin filaments". Journal of Cell Science. 128 (11): 2009–19. doi:10.1242/jcs.165563. PMID 25788699.
^Ghoshdastider U, Jiang S, Popp D, Robinson RC (Jul 2015). "In search of the primordial actin filament". Proceedings of the National Academy of Sciences of the United States of America. 112 (30): 9150–1. doi:10.1073/pnas.1511568112. PMC 4522752. PMID 26178194.
^Szwedziak P, Wang Q, Freund SM, Löwe J (May 2012). "FtsA forms actin-like protofilaments". The EMBO Journal. 31 (10): 2249–60. doi:10.1038/emboj.2012.76. PMC 3364754. PMID 22473211.
^Pichoff S, Shen B, Sullivan B, Lutkenhaus J (Jan 2012). "FtsA mutants impaired for self-interaction bypass ZipA suggesting a model in which FtsA's self-interaction competes with its ability to recruit downstream division proteins". Molecular Microbiology. 83 (1): 151–67. doi:10.1111/j.1365-2958.2011.07923.x. PMC 3245357. PMID 22111832.
^Karuppiah V, Derrick JP (Jul 2011). "Structure of the PilM-PilN inner membrane type IV pilus biogenesis complex from Thermus thermophilus". The Journal of Biological Chemistry. 286 (27): 24434–42. doi:10.1074/jbc.M111.243535. PMC 3129222. PMID 21596754.
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