MULTISPECIES: type VI secretion system contractile sheath small subunit [Enterobacter]
type VI secretion system contractile sheath small subunit( domain architecture ID 10007505)
type VI secretion system contractile sheath small subunit TssB/VipA assembles with the large subunit TssC/VipB to form tubules that conserve structural/functional homology with tail sheaths of contractile bacteriophages and pyocins
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
TssB | COG3516 | Predicted component TssA of the type VI protein secretion system [Intracellular trafficking, ... |
3-172 | 2.84e-91 | ||||
Predicted component TssA of the type VI protein secretion system [Intracellular trafficking, secretion, and vesicular transport]; : Pssm-ID: 442738 Cd Length: 171 Bit Score: 263.20 E-value: 2.84e-91
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Name | Accession | Description | Interval | E-value | ||||
TssB | COG3516 | Predicted component TssA of the type VI protein secretion system [Intracellular trafficking, ... |
3-172 | 2.84e-91 | ||||
Predicted component TssA of the type VI protein secretion system [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 442738 Cd Length: 171 Bit Score: 263.20 E-value: 2.84e-91
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T6SS_VipA | pfam05591 | Type VI secretion system, VipA, VC_A0107 or Hcp2; T6SSs are toxin delivery systems. It is a ... |
11-161 | 1.29e-75 | ||||
Type VI secretion system, VipA, VC_A0107 or Hcp2; T6SSs are toxin delivery systems. It is a multiprotein complex requiring numerous core proteins (Tss proteins) including cytoplasmic, transmembrane, and outer membrane components. The needle or tube apparatus is comprised of a phage-like complex, similar to the T4 contractile bacteriophage tail, which is thought to be anchored to the membrane by a trans-envelope complex. VipA is a family of Gram-negative bacterial proteins that form part of the type VI pathogenic secretion system. Members have been variously defined as VC_A0107 family, Hcp2, TssB and VipA, for ClpV-interacting proteins. VipB and VipA proteins interact very closely to form the shaft of the pathogenic penetrating needle system. VipA and VipB (TssB and TssC) proteins were shown to form a cog-wheel like tubular structure in V. cholerae that was noticed to resemble T4 phage gp18 polysheath. Two beta-strands of VipA and four beta-strands of VipB intertwine forming the middle layer of the sheath. The sheath assembles around an inner Hcp tube and is attached to a structure called a baseplate that spans the bacterial membranes. Importantly, VipA/VipB sheath was shown to form a long contractile organelle in V. cholerae and in E. coli, suggesting that sheath contraction powers the secretion. Pssm-ID: 428529 Cd Length: 154 Bit Score: 223.11 E-value: 1.29e-75
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VI_chp_5 | TIGR03358 | type VI secretion protein, VC_A0107 family; Work by Mougous, et al. (2006), describes ... |
9-164 | 1.41e-69 | ||||
type VI secretion protein, VC_A0107 family; Work by Mougous, et al. (2006), describes IAHP-related loci as a type VI secretion system (). This protein family is associated with type VI secretion loci, although not treated explicitly by Mougous, et al. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis] Pssm-ID: 132401 Cd Length: 159 Bit Score: 207.90 E-value: 1.41e-69
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Name | Accession | Description | Interval | E-value | ||||
TssB | COG3516 | Predicted component TssA of the type VI protein secretion system [Intracellular trafficking, ... |
3-172 | 2.84e-91 | ||||
Predicted component TssA of the type VI protein secretion system [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 442738 Cd Length: 171 Bit Score: 263.20 E-value: 2.84e-91
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T6SS_VipA | pfam05591 | Type VI secretion system, VipA, VC_A0107 or Hcp2; T6SSs are toxin delivery systems. It is a ... |
11-161 | 1.29e-75 | ||||
Type VI secretion system, VipA, VC_A0107 or Hcp2; T6SSs are toxin delivery systems. It is a multiprotein complex requiring numerous core proteins (Tss proteins) including cytoplasmic, transmembrane, and outer membrane components. The needle or tube apparatus is comprised of a phage-like complex, similar to the T4 contractile bacteriophage tail, which is thought to be anchored to the membrane by a trans-envelope complex. VipA is a family of Gram-negative bacterial proteins that form part of the type VI pathogenic secretion system. Members have been variously defined as VC_A0107 family, Hcp2, TssB and VipA, for ClpV-interacting proteins. VipB and VipA proteins interact very closely to form the shaft of the pathogenic penetrating needle system. VipA and VipB (TssB and TssC) proteins were shown to form a cog-wheel like tubular structure in V. cholerae that was noticed to resemble T4 phage gp18 polysheath. Two beta-strands of VipA and four beta-strands of VipB intertwine forming the middle layer of the sheath. The sheath assembles around an inner Hcp tube and is attached to a structure called a baseplate that spans the bacterial membranes. Importantly, VipA/VipB sheath was shown to form a long contractile organelle in V. cholerae and in E. coli, suggesting that sheath contraction powers the secretion. Pssm-ID: 428529 Cd Length: 154 Bit Score: 223.11 E-value: 1.29e-75
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VI_chp_5 | TIGR03358 | type VI secretion protein, VC_A0107 family; Work by Mougous, et al. (2006), describes ... |
9-164 | 1.41e-69 | ||||
type VI secretion protein, VC_A0107 family; Work by Mougous, et al. (2006), describes IAHP-related loci as a type VI secretion system (). This protein family is associated with type VI secretion loci, although not treated explicitly by Mougous, et al. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis] Pssm-ID: 132401 Cd Length: 159 Bit Score: 207.90 E-value: 1.41e-69
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