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Conserved domains on  [gi|268327069|dbj|BAI49510|]
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MobB [Shuttle vector pYN401]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Mobilization_B super family cl38782
Mobilization protein B; This is a family of unknown function found in Bacteria. Family members ...
 1-132 2.23e-39

Mobilization protein B; This is a family of unknown function found in Bacteria. Family members include Mobilization protein B (MobB). MobB contains a putative membrane-spanning domain, and might be involved in anchoring or presenting MobA, and the covalently-linked plasmid DNA, to the conjugative pore for subsequent export. In agreement with this, MobB has been shown to be associated with the membrane. Deletion of the membrane-spanning domain disrupts this association and decreases the frequency of both type IV transport and plasmid mobilization. MobB is one out of three proteins encoded by RSF1010 that are required for its mobilization along with MobA and MobC. MobB encoded by the broad-host-range plasmid R1162 is required for its efficient transfer by conjugation. The C-terminal half of the protein contains a membrane domain essential for transfer, while the other, functionally active region of MobB, identified by mutagenesis, is at the N-terminal end. One mutation affecting this region inhibits replication, suggesting that this part of the protein is contacting and sequestering the relaxase-linked primase. A model that represents MobB molecules as anchored in the membrane at one end and engaging the relaxase at the other. This arrangement is suggested to increase the transfer frequency by raising the probability of contact between the relaxase and the membrane-embedded, coupling protein for type IV secretion.


The actual alignment was detected with superfamily member pfam17511:

Pssm-ID: 340226  Cd Length: 136  Bit Score: 129.11  E-value: 2.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268327069    1 MNAIDRVKKSRGINELAEQIEPLAQSMATLADEARQVMSQTQQASEAQAAEWLKAQRQTGAAWVELAKELREVAAEVSSA 80
Cdd:pfam17511   1 MSAIDRVKKSRGINELAAEIEPLAQSMATLADEARQRIAETQQASEAQAAEWLKAQQQAGAAWREAAKDLRAAAAELAKA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 268327069   81 AQSARSASRGWHWKLWLTVMLASMMPtVVLLIASLLLLDLTPLTTEDGSIWL 132
Cdd:pfam17511  81 AQSARSAARGWTWKLWAGVLIASVMP-ILALLIASWLWLEPQIIEQQGGIWL 131
 
Name Accession Description Interval E-value
Mobilization_B pfam17511
Mobilization protein B; This is a family of unknown function found in Bacteria. Family members ...
 1-132 2.23e-39

Mobilization protein B; This is a family of unknown function found in Bacteria. Family members include Mobilization protein B (MobB). MobB contains a putative membrane-spanning domain, and might be involved in anchoring or presenting MobA, and the covalently-linked plasmid DNA, to the conjugative pore for subsequent export. In agreement with this, MobB has been shown to be associated with the membrane. Deletion of the membrane-spanning domain disrupts this association and decreases the frequency of both type IV transport and plasmid mobilization. MobB is one out of three proteins encoded by RSF1010 that are required for its mobilization along with MobA and MobC. MobB encoded by the broad-host-range plasmid R1162 is required for its efficient transfer by conjugation. The C-terminal half of the protein contains a membrane domain essential for transfer, while the other, functionally active region of MobB, identified by mutagenesis, is at the N-terminal end. One mutation affecting this region inhibits replication, suggesting that this part of the protein is contacting and sequestering the relaxase-linked primase. A model that represents MobB molecules as anchored in the membrane at one end and engaging the relaxase at the other. This arrangement is suggested to increase the transfer frequency by raising the probability of contact between the relaxase and the membrane-embedded, coupling protein for type IV secretion.


Pssm-ID: 340226  Cd Length: 136  Bit Score: 129.11  E-value: 2.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268327069    1 MNAIDRVKKSRGINELAEQIEPLAQSMATLADEARQVMSQTQQASEAQAAEWLKAQRQTGAAWVELAKELREVAAEVSSA 80
Cdd:pfam17511   1 MSAIDRVKKSRGINELAAEIEPLAQSMATLADEARQRIAETQQASEAQAAEWLKAQQQAGAAWREAAKDLRAAAAELAKA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 268327069   81 AQSARSASRGWHWKLWLTVMLASMMPtVVLLIASLLLLDLTPLTTEDGSIWL 132
Cdd:pfam17511  81 AQSARSAARGWTWKLWAGVLIASVMP-ILALLIASWLWLEPQIIEQQGGIWL 131
 
Name Accession Description Interval E-value
Mobilization_B pfam17511
Mobilization protein B; This is a family of unknown function found in Bacteria. Family members ...
 1-132 2.23e-39

Mobilization protein B; This is a family of unknown function found in Bacteria. Family members include Mobilization protein B (MobB). MobB contains a putative membrane-spanning domain, and might be involved in anchoring or presenting MobA, and the covalently-linked plasmid DNA, to the conjugative pore for subsequent export. In agreement with this, MobB has been shown to be associated with the membrane. Deletion of the membrane-spanning domain disrupts this association and decreases the frequency of both type IV transport and plasmid mobilization. MobB is one out of three proteins encoded by RSF1010 that are required for its mobilization along with MobA and MobC. MobB encoded by the broad-host-range plasmid R1162 is required for its efficient transfer by conjugation. The C-terminal half of the protein contains a membrane domain essential for transfer, while the other, functionally active region of MobB, identified by mutagenesis, is at the N-terminal end. One mutation affecting this region inhibits replication, suggesting that this part of the protein is contacting and sequestering the relaxase-linked primase. A model that represents MobB molecules as anchored in the membrane at one end and engaging the relaxase at the other. This arrangement is suggested to increase the transfer frequency by raising the probability of contact between the relaxase and the membrane-embedded, coupling protein for type IV secretion.


Pssm-ID: 340226  Cd Length: 136  Bit Score: 129.11  E-value: 2.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 268327069    1 MNAIDRVKKSRGINELAEQIEPLAQSMATLADEARQVMSQTQQASEAQAAEWLKAQRQTGAAWVELAKELREVAAEVSSA 80
Cdd:pfam17511   1 MSAIDRVKKSRGINELAAEIEPLAQSMATLADEARQRIAETQQASEAQAAEWLKAQQQAGAAWREAAKDLRAAAAELAKA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 268327069   81 AQSARSASRGWHWKLWLTVMLASMMPtVVLLIASLLLLDLTPLTTEDGSIWL 132
Cdd:pfam17511  81 AQSARSAARGWTWKLWAGVLIASVMP-ILALLIASWLWLEPQIIEQQGGIWL 131
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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