Literature summary for 7.2.2.5 extracted from

Colomer-Winter, C.; Flores-Mireles, A.; Baker, S.; Frank, K.; Lynch, A.; Hultgren, S.; Kitten, T.; Lemos, J.
Manganese acquisition is essential for virulence of Enterococcus faecalis (2018), PLoS Pathog., 14, e1007102 .

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Organism

Organism	UniProt	Comment	Textmining
Enterococcus faecalis	Q832Z4 and Q832Z3 and Q832Z2	Q832Z4 i.e. ATP-binding protein EfaC, Q832Z3 i.e. permease protein EfaB, Q832Z2 i.e. subunit EfaA	-
Enterococcus faecalis ATCC 700802	Q832Z4 and Q832Z3 and Q832Z2	Q832Z4 i.e. ATP-binding protein EfaC, Q832Z3 i.e. permease protein EfaB, Q832Z2 i.e. subunit EfaA	-

Synonyms

Synonyms	Comment	Organism
EF_2074	-	Enterococcus faecalis
EF_2075	-	Enterococcus faecalis
EF_2076	-	Enterococcus faecalis

General Information

General Information	Comment	Organism
physiological function	ABC-type permease EfaCBA and Nramp-type transporters, MntH1 and MntH2, work collectively to promote cell growth under Mn-restricted conditions. The simultaneous inactivation of EfaCBA, MntH1 and MntH2 leads to more than 95% reductions in cellular Mn content, severe growth defects in serum and urine ex vivo, significant loss of virulence in Galleria mellonella, and virtually complete loss of virulence in rabbit endocarditis and murine catheter-associated urinary tract infection models. Dual inactivation of EfaCBA and MntH2 is sufficient to prompt maximal sensitivity to calprotectin, and for the loss of virulence in mammalian models	Enterococcus faecalis

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Release 2023.1 (January 2023)