EfeM/EfeO family lipoprotein similar to the iron uptake system component EfeM, which is part of a ferrous iron transporter composed of EfeU, EfeM, and EfeN
EfeO is a component of the EfeUOB operon; This family includes the EfeO domain, an essential ...
41-280
8.09e-105
EfeO is a component of the EfeUOB operon; This family includes the EfeO domain, an essential component of the EfeUOB operon which is highly conserved in bacteria. However, its biochemical function is unknown. EfeO contains an N-terminal cupredoxin (CUP)-like domain and C-terminal imelysin-like domain that may bind iron. Algp7, a member of EfeO family protein from Sphingomonas sp. A1, is found to bind alginate at neutral pH, but does not contain the CUP domain, thus having a role that does not seem to be related to iron uptake. Some members of this family are fused to an N-terminal putative EfeU ion permease domain. The imelysin-like domain of this family also contains the GxHxxE sequence motif and a highly conserved functional site, suggesting a similar role to other imelysin family proteins containing the same motif.
Pssm-ID: 271139 Cd Length: 239 Bit Score: 304.56 E-value: 8.09e-105
Imelysin; The imelysin peptidase was first identified in Pseudomonas aeruginosa. The active ...
47-279
3.99e-31
Imelysin; The imelysin peptidase was first identified in Pseudomonas aeruginosa. The active site residues have not been identified. However, His201 and Glu204 are completely conserved in the family and occur in an HXXE motif that is also found in family M14.
Pssm-ID: 430568 Cd Length: 289 Bit Score: 117.17 E-value: 3.99e-31
EfeO is a component of the EfeUOB operon; This family includes the EfeO domain, an essential ...
41-280
8.09e-105
EfeO is a component of the EfeUOB operon; This family includes the EfeO domain, an essential component of the EfeUOB operon which is highly conserved in bacteria. However, its biochemical function is unknown. EfeO contains an N-terminal cupredoxin (CUP)-like domain and C-terminal imelysin-like domain that may bind iron. Algp7, a member of EfeO family protein from Sphingomonas sp. A1, is found to bind alginate at neutral pH, but does not contain the CUP domain, thus having a role that does not seem to be related to iron uptake. Some members of this family are fused to an N-terminal putative EfeU ion permease domain. The imelysin-like domain of this family also contains the GxHxxE sequence motif and a highly conserved functional site, suggesting a similar role to other imelysin family proteins containing the same motif.
Pssm-ID: 271139 Cd Length: 239 Bit Score: 304.56 E-value: 8.09e-105
imelysin also called Peptidase M75; This family includes insulin-cleaving membrane protease ...
43-279
1.26e-31
imelysin also called Peptidase M75; This family includes insulin-cleaving membrane protease (imelysin, ICMP), imelysin-like protein (IPPA from Psychrobacter arcticus), iron-regulated protein A (IrpA) and iron-transporter EfeO-like alginate-binding protein (Algp7). Imelysin is a membrane protein with the active site outside the cell envelope. It is also called the peptidase M75 since the HxxE sequence motif characteristic of the M14 peptidase is completely conserved. However, the overall structure and the GxHxxE motif region differ from the known HxxE metallopeptidases, suggesting that imelysin-like proteins may not be peptidases. Imelysin's cleavage of the oxidized insulin B chain shows a preference for aromatic hydrophobic amino acids at P1'. Imelysin was first identified in Pseudomonas aeruginosa and has also been shown to cleave fibrinogen. The tertiary structure shows a fold consisting of two domains, each consisting of a bundle of four helices that are similar to each other, implying an ancient gene duplication and fusion event. In addition to an imelysin-like domain, Algp7 typically contains an N-terminal cupredoxin (CUP) domain and has a deep cleft between the 4-helix bundles sufficiently large to accommodate macromolecules such as alginate polysaccharide.
Pssm-ID: 271138 Cd Length: 253 Bit Score: 117.72 E-value: 1.26e-31
Imelysin; The imelysin peptidase was first identified in Pseudomonas aeruginosa. The active ...
47-279
3.99e-31
Imelysin; The imelysin peptidase was first identified in Pseudomonas aeruginosa. The active site residues have not been identified. However, His201 and Glu204 are completely conserved in the family and occur in an HXXE motif that is also found in family M14.
Pssm-ID: 430568 Cd Length: 289 Bit Score: 117.17 E-value: 3.99e-31
Imelysin-like domain in iron-regulated protein A; This family includes putative iron-regulated ...
62-278
6.77e-15
Imelysin-like domain in iron-regulated protein A; This family includes putative iron-regulated protein A (IrpA) mainly from Bacteriodes, proteobacteria and cyanobacteria, with domain similar to insulin-cleaving membrane protease (imelysin, ICMP) protein. It has been shown to be essential for growth under iron-deficient conditions in the cyanobacteria Synechococcus sp. The conserved GxHxxE motif is similar to other known imelysin-like proteins that are regulated by iron, such as ICMP, IrpA and EfeO. Imelysin is a membrane protein with the active site outside the cell envelope. The tertiary structure shows a fold consisting of two domains, each of which consists of a bundle of four helices that are similar to each other, implying an ancient gene duplication and fusion event.
Pssm-ID: 271141 Cd Length: 282 Bit Score: 73.06 E-value: 6.77e-15
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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